Journal of clinical pathology. Supplement (Association of Clinical Pathologists)最新文献

{"title":"Vasoactive intestinal peptide (VIP).","authors":"M G Bryant","doi":"10.1136/jcp.s1-8.1.63","DOIUrl":"https://doi.org/10.1136/jcp.s1-8.1.63","url":null,"abstract":"In 1969, Said and Mutt reported the extraction from secretion, increased flow of alkaline pancreatic normal lung tissue of a peptide which was capable juice and small intestinal juice with increased cyclic of causing gradual but prolonged peripheral AMP content (Makhlouf and Said, 1975), overlap vasodilation. This finding led them to search for markedly with the actions of the other three peptides. similar vasoactive substances in extracts of other Thus VIP was included as a member of the secretin metabolically active organs and, in 1970, they family ofhormonal peptides and, in 1974, it appeared described the isolation of a potent peripheral and in a list of 'candidate hormones of the gut' compiled splanchnic vasodilatory peptide from hog small by Grossman et al. (1974). intestine, which they named Vasoactive Intestinal In the eight or so years since its discovery, a great Peptide (VIP) (Said and Mutt, 1970 a, b). Subsequent deal of information has been amassed about VIP. purification of VIP allowed determination of its With the development of highly sensitive and specific amino-acid sequence, which showed it to be a radioimmunoassays for VIP, it has been possible to straight chain of 28 amino-acid residues with basic study its distribution in the body and its mode of properties because of a predominance of arginine release. However, with this growth in knowledge and lysine residues (Said and Mutt, 1972). Comparicontroversy developed as to whether VIP fulfilled son of the amino-acid sequence of VIP with those of the classical criteria for a hormone or whether it the classical hormones secretin and pancreatic acted locally as a paracrine substance or even as a glucagon showed a considerable degree of homology neurotransmitter or neuromodulatory substance. (Fig. 1). Thus, these three peptides, together with the This has now been resolved in favour of the latter, more recently discovered glucose-dependent insulin as discussed below. releasing polypeptide (GIP), were thought to be Perhaps one of the first indications that VIP related and it was suggested that they were perhaps might not be a hormone was obtained -from its derived from a common ancestral peptide. Further distribution in the gut. Unlike the other members of weight was added to these suggestions by the fact the secretin family, which are located in discrete that the many biological effects of VIP, which regions of the upper small intestine (secretin) and include systemic vasodilation, glycogenolysis (Kerins pancreas (glucagon), VIP appeared to have a much and Said, 1973), lipolysis (Frandsen and Moody, wider distribution. High concentrations of VIP were' 1973), inhibition of gastric acid production found throughout the length of the gut from the (Makhlouf and Said, 1975), stimulation of oesophagus to the rectum, including the pancreas myocardial contractility (Said et al., 1972), insulin (Bloom et al., 1975; Said, 1975) (Fig. 2). A similar *Serum is [unsuitable for VIP estimations as th","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"8 ","pages":"63-7"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-8.1.63","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11510377","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Gut glucagon-like immunoreactants (GLIs) and other enteric glucagon-like peptides.","authors":"A J Moody","doi":"10.1136/jcp.s1-8.1.58","DOIUrl":"https://doi.org/10.1136/jcp.s1-8.1.58","url":null,"abstract":"The term glucagon was coined by Kimball and an immunoreactant in common with glucagon (gut Murlin (1923) to describe a hyperglycaemic subGLIs). The extensive similarities between the stance which they had partially purified from an sequences of glucagon, VIP, secretin, and GIP have extract of bovine pancreas. In 1953, Staub et al. been discussed elsewhere in these proceedings. The crystallised a pancreatic hyperglycaemic glycofour peptides have very similar spectra of biological genolytic factor (HGF), for which they accepted the effects: secretin, glucagon, and VIP stimulate name glucagon in 1955 (Staub et al., 1955). The lipolysis, VIP and glucagon activate glycogenolysis, amino-acid sequence of porcine glucagon was and all of the peptides are insulin-releasing in one published in 1956 by Bromer et al. With the excepsystem or another (see Marks and Turner, 1977 for tion of guinea pig glucagon, all mammalian glua review). These effects are probably all exerted via cagons so far isolated have the same 29 amino-acid stimulation of adenyl cyclase but involve binding of sequence as porcine glucagon (Sundby, 1976). the peptides to separate receptors on the cell surface. Avian glucagons differ from porcine glucagon; for The physiology of secretin, VIP, and GIP is described example turkey glucagon differs by having a serine elsewhere in these proceedings so the remainder of residue at position 28 instead of asparagine, and this section is restricted to the gut glucagon-like duck glucagon by also having a threonine at position immunoreactants (gut GLIs). 16 instead of serine (Fig. 1). In the mammals studied so far, glucagon has been located mainly in the Gut glucagon-like immunoreactants pancreas, where it is synthesised in the A cells of the islets of Langerhans (Bussolati et al., 1971). A well The term gut glucagon-like immunoreactant is used characterised gastric glucagon has, however, been for any gut peptide which reacts with an antilocated in A-like cells in the canine gastric mucosa glucagon serum to prevent the binding of radio(Vranic et al., 1976). iodinated glucagon to the antibodies in the serum. The first description of a substance in the gastroThe existence of gut GLIs and the pattern of their intestinal tract with glucagon-like activities was secretion by the intestine was shown in the 1960s, the demonstration by Sutherland and de Duve largely by Unger and co-workers (1968). They react (1948) of a hyperglycaemic-glycogenolytic factor in with only one type of anti-glucagon serum, variously the canine upper gastrointestinal tract. This presentaknown as non-specific, cross-reacting, or N terminal tion summarises our knowledge of those glucagonspecific (see immunochemistry below). like peptides which have been isolated from enteric Long-chain triglycerides and glucose have been tissues since this first report. shown to release gut GLIs, as has the ingestion of Enteric peptides can be considered to be glucagonmixed meals (see Bloom and Polak, 1","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"8 ","pages":"58-62"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-8.1.58","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11510376","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Gut hormones in gastrointestinal disease.","authors":"H S Besterman","doi":"10.1136/jcp.s1-8.1.76","DOIUrl":"https://doi.org/10.1136/jcp.s1-8.1.76","url":null,"abstract":"Considerable advances have been made in the understanding of the physiology of gut hormones. Thus, knowledge of the mechanisms of release and of the actions of many of the hormones is rapidly expanding. The known clinical importance of gut hormones is at present confined only to the excess production of gastrin, VIP, and pancreatic glucagon by endocrine tumours. The role of these three and the other gut hormones in disease states affecting the pancreas and gut has been studied little. Investigation of the patterns of gut hormone release in alimentary disease may provide new insight into the pathophysiology of these disorders. Not only may gut hormones be implicated as primary agents in the pathological processes, but also secondary changes in gut hormone release may be related to compensatory and adaptive mechanisms. Further insight may also be gained into the normal physiological roles of the hormones themselves through the effects of diminished or augmented release found in gut diseases. We have, therefore, studied the gut hormone profile after a normal meal in several well defined gastrointestinal diseases, with features summarised in Table 1. The distribution of the known gut hormones has been elucidated by the combined techniques of quantitative immunocytochemistry and radioimmunoassay of extracted tissues (Bloom et al., 1975; Bryant and Bloom, 1979). The hormones have characteristic locations which are summarised in Table 2. Diseases affect the alimentary tract in many different ways, some of them affecting only certain portions of the gut. It is to be expected that the release ofgut hormones from areas damaged by the disease would be abnormal. The release of other hormones from areas of bowel uninvolved in disease, however, might also show secondary changes. The plasma levels of most gut hormones rise substantially after food. Thus the stimulus to hormone release used in studying the various disease states was a 'physiological' test breakfast. This consisted of two medium-sized boiled eggs, 10 g butter, 60 g bread as toast, 35 g marmalade, and Disease or Area mavimally Clinical and pathological state affected pathologicalfeatures","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"8 ","pages":"76-84"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-8.1.76","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11513639","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The endocrine versatility of the gut: general and evolutionary aspects of the active peptides of the gastrointestinal tract.","authors":"G J Dockray","doi":"10.1136/jcp.s1-8.1.1","DOIUrl":"https://doi.org/10.1136/jcp.s1-8.1.1","url":null,"abstract":"Recent years have seen an unprecedented expansion of interest in the gastrointestinal endocrine system that shows no signs of abating. In large measure this awakening can be attributed to the chemical studies that have resulted in the isolation and elucidation of structure of a wide variety of biologically active gut peptides (Gregory and Tracy, 1975; Mutt, 1976). The availability of highly purified preparations of these peptides has made possible detailed studies of their effects and mode of action at the cellular level. In addition, it has become possible to apply immunochemical methods of analysis that have helped to reveal the cellular origins of the peptides and have allowed their estimation in blood and tissue extracts. Several unexpected findings have emerged from these studies. For example, it now seems possible that some of the peptides produced by gut endocrine cells are not secreted into the blood stream, but rather act locally by diffusion to their targets through the extracellular space (paracrine effects). Furthermore, it is now clear that many of the active peptides in gut extracts originate not just in gut endocrine cells but also in nerve fibres. Peptides of the enteric plexuses are also found in the central nervous system, and other peptides previously identified in brain have since been found in the gut. These developments raise questions of fundamental importance about the interrelationships of the brain-gut peptides and their roles in health and disease that, taken together, point to the need for a re-evaluation of the system of peptide messengers as a whole. An important aspect of such an analysis is the extent to which the chemical and functional relationships of these peptides can be accounted for in evolutionary terms. The relevance of this approach is emphasised by the similarity in structure of groups of brain-gut peptides that suggest a shared ancestry, both of the molecules in question, and of the entire system of neuronal and hormonal peptides.","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"8 ","pages":"1-6"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-8.1.1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11447555","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pathophysiology of gastrin and secretin.","authors":"K D Buchanan, J E Ardill","doi":"10.1136/jcp.s1-8.1.17","DOIUrl":"https://doi.org/10.1136/jcp.s1-8.1.17","url":null,"abstract":"This paper will attempt to define the pathological roles of gastrin and secretin. It will deal predominantly with gastrin which now has an accepted role in some diseases, whereas the pathological role of secretin has still to emerge. Basic physiology and chemistry will only be described where these are considered to be relevant to the interpretation of the roles of these hormones in disease.","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"8 ","pages":"17-25"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-8.1.17","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11605731","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The enteroinsular axis.","authors":"V Marks","doi":"10.1136/jcp.s1-8.1.38","DOIUrl":"https://doi.org/10.1136/jcp.s1-8.1.38","url":null,"abstract":"Rediscovery of the role of the gastrointestinal tract in the control of carbohydrate metabolism and, as we now know, fat and protein metabolism, was made independently in London by two groups of workers (Dupre, 1964a; McIntyre et al., 1964). The major credit undoubtedly belongs to McIntyre and his colleagues (1964, 1965) who, by the simplest of methods, namely comparing the glycaemic and insulinaemic responses to equal amounts of glucose given by intravenous and intrajejunal infusion, and using only two subjects initially, were able to show that the gut mediated an augmentation of the insulinaemic response to hyperglycaemia. Despite an enormous amount of effort by many workers since that time, it is still not possible to attribute, with any degree of certainty, the role of intestinal augmenter of glucose-stimulated insulin release to any one agency. Nervous factors undoubtedly play a role but will not be considered here. Of the many hormonal agents that have been proposed, some meet the bill better than others. For the sake of brevity I shall exclude from further consideration those which I believe play only a minor or non-existent role and concentrate upon those substances that I have personally been most concerned with or consider to be potentially physiologically important, namely glucagon, gut glucagon-cross-reacting material, or GLI (often, perhaps inappropriately, referred to as enteroglucagon), insulin-releasing polypeptide (IRP) and GIP.' Several comprehensive reviews are available and interested readers are referred to them (Marks and Samols, 1970; Marks and Turner, 1977).","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"8 ","pages":"38-42"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-8.1.38","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11605733","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Visualisation of the diffuse endocrine system.","authors":"I M Dawson","doi":"10.1136/jcp.s1-8.1.7","DOIUrl":"https://doi.org/10.1136/jcp.s1-8.1.7","url":null,"abstract":"Bacon declared that 'the informed mind is more apt to see'; in the matter of detecting endocrine cells within the gastrointestinal tract, though some 400 years in advance of his time, he was correct. Endocrine cells are distinguishable from other gastrointestinal epithelial cells by the presence within their cytoplasm of secretory granules, and with due care and expectation of their presence these may often be recognised in conventionally stained paraffin embedded material, as many 19th and early 20th century histologists appreciated (see Clara, 1957). Not all endocrine cells, however, have granules which are recognisable, nor is differentiation between the shape and content of one granule and another possible on conventional haematoxylin and eosin staining. The purpose of this presentation is briefly to review the different types of endocrine cell found in the gut and the techniques by which one may be separated from another (Dawson, 1970, 1976). Endocrine cells in the gut are constructed as variants on a common pattern. They tend to be pear shaped or triangular, with a broad base abutting onto the basement membrane and a narrow apex which usually reaches the intestinal lumen and often bears microvilli. There is a conspicuous rough endoplasmic reticulum and Golgi, and mitochondria rich in decarboxylases and esterases. The most significant feature, however, is the presence within the cytoplasm of storage granules surrounded by a lipoprotein envelope, which tend to be especially numerous at the base rather than at the apex of each cell. Endocrine cells are classified by the content of these granules which can potentially be determined either by histochemical or by immunocytological techniques. Since granule size, shape, and density also seem to be related to granular content, ultrastructural studies may afford a separate means of identifying cell function. The granules in most endocrine cells in the gut contain a polypeptide hormone. Some contain an identifiable biological amine of which 5-hydroxytryptamine (SHT) is the most important. It is the supposed ability of all endocrine cells to be able to decarboxylate amine precursors which has led to their being referred to as APUD (Amine Precursor Uptake and Decarboxylation) cells, a term which 7 Pearse and his co-workers have enthusiastically embraced in their many detailed studies of an evergrowing family (Pearse, 1968, 1969). Since not all cells which secrete polypeptide hormones can be shown to decarboxylate and store amine precursors, I prefer the non-committal term endocrine cells; certainly endocrine cell tumour, when the precise secretion (for example, insulinoma) cannot be named, is preferable to the ugly word Apudoma.","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"8 ","pages":"7-11"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-8.1.7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11316104","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The measurement of cholecystokinin.","authors":"J F Rehfeld","doi":"10.1136/jcp.s1-8.1.26","DOIUrl":"https://doi.org/10.1136/jcp.s1-8.1.26","url":null,"abstract":"Measurement of hormones in biological fluids is an obvious prerequisite for evaluation of their physiological and pathophysiological significance. Of the steadily increasing list of gastrointestinal hormones, cholecystokinin (CCK) was the third to be discovered (Ivy and Oldberg, 1928). Cholecystokinin, secretin, and gastrin constitute the classical triad of gut hormones which, until recently, was assumed to exert the entire humoral control of digestion (Grossman, 1970a). While it is now possible to measure the plasma concentration of gastrin, secretin, and most of the other chemically defined hormonal peptides from the gut (reviewed by Rehfeld, 1978a), all attempts to measure CCK in plasma have, in the author's opinion, failed. An interest in the molecular nature of gastrin and gastrin-like peptides, and experience of assays for a number of gastrointestinal and other hormones, led me to establish the radioimmunoassay of CCK. After initial difficulties with the labelling of CCK had been overcome, sensitive and sequence-specific radioimmunoassays for CCK were developed (Rehfeld, 1978b). However, for several reasons, these assays proved unsatisfactory when applied to plasma. As foreseen several years ago using crossreacting gastrin assays (unpublished data), CCK occurs in several forms and their concentration in plasma is very low. Moreover, plasma proteins interfere greatly in the assay, and some plasma enzymes probably degrade CCK. These problems still have to be overcome. Nevertheless, it is hoped that the following account may be of some value.","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"8 ","pages":"26-30"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-8.1.26","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11510373","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Brain and gut peptides.","authors":"J M Polak","doi":"10.1136/jcp.s1-8.1.68","DOIUrl":"https://doi.org/10.1136/jcp.s1-8.1.68","url":null,"abstract":"The first evidence that the same peptides could be present in both the brain and the gut was given in 1931 with the discovery of substance P (Von Euler and Gaddum, 1931). In spite of this early start, the important revelation that there were a large number of peptides with this dual localisation and also with powerful and extensive pharmacological actions took more than 40 years to materialise. After the finding of large quantities of the hypothalamic peptide somatostatin (Arimura et al., 1975) in the gastrointestinal tract, increasing numbers of peptides have been found to be common to the gut and brain. To date the list includes somatostatin, substance P, cholecystokinin (CCK), enkephalin, neurotensin, vasoactive intestinal polypeptide (VIP), and bombesin. A number of these peptides, such as somatostatin, neurotensin, and enkephalin, were originally found in the brain and later in the gut, whereas others, such as VIP, bombesin, and gastrin, were found first in the gut. There is increasing evidence that outside the brain these peptides are localised in typical endocrine cells, or in fine efferent nerve fibres, or both, as part of the autonomic innervation. Although some peptides","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"8 ","pages":"68-75"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-8.1.68","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11316103","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pancreatic polypeptide.","authors":"T E Adrian","doi":"10.1136/jcp.s1-8.1.43","DOIUrl":"https://doi.org/10.1136/jcp.s1-8.1.43","url":null,"abstract":"Pancreatic polypeptide (PP) was discovered fortuitously during the purification of insulin from birds (Kimmel et al., 1968) and later from mammals (Chance et al., 1976). PP has since been extracted and purified from several mammalian species. It contains 36 amino-acid residues and is quite distinct from other known hormonal peptides (Lin and Chance, 1974). The amino-acid sequence of the peptides extracted from man, pig, dog, sheep, and cow differs only in one or two residues in positions 2, 6, or 23 (Lin and Chance, 1974). The biological activity of these mammalian peptides has been found to reside in the C terminal hexapeptide (Lin and Chance, 1978). Rodent PP, however, appears to be somewhat different in that it does not cross-react with the majority of antisera raised to the bovine peptide.","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"8 ","pages":"43-50"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-8.1.43","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11510374","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}