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

{"title":"Protein profiles derived by automated immune precipitation.","authors":"R F Ritchie","doi":"10.1136/jcp.s1-6.1.27","DOIUrl":"https://doi.org/10.1136/jcp.s1-6.1.27","url":null,"abstract":"This presentation will cover much the same ground as Professor Laurell's but from a slightly different viewpoint. There is no great difference between us, though we use agarose gel electrophoresis only to detect paraproteins. Like others, we feel that scanning the electrophoretogram contributes nothing to the interpretation of the test', as even with high resolution systems the various fractions are composed of mixtures. Instead, we prefer to estimate specific proteins by the automated immunoprecipitation system, and we routinely estimate 12 plasma proteins (albumin, ctl-antitrypsin, haptoglobin, oro-somucoid, ct2-macroglobulin, transferrin, complement C3, complement C4, IgG, IgA, IgM, LDL protein) and can estimate more than 30. The same proteins could of course be estimated by the techniques outlined by Dr Laurell. Specific protein analysis is superior to electrophoresis in that in","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"6 ","pages":"27-32"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-6.1.27","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12258021","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":"gamma- and mu-Heavy chain diseases and related disorders.","authors":"E C Franklin","doi":"10.1136/jcp.s1-6.1.65","DOIUrl":"https://doi.org/10.1136/jcp.s1-6.1.65","url":null,"abstract":"During the last ten years studies of myeloma proteins have shown them to be similar to or identical with normal immunoglobulins. In addition, the not infrequent occurrence of structural variants of immunoglobulins in association with neoplasms of lymphocytes or plasma cells has become widely recognized. Since the discovery of the group of heavy chain diseases in man (Franklin, Meltzer, Guggenheim, and Lowenstein, 1963; Franklin, Lowenstein, Bigelow, and Meltzer, 1964) and shortly afterwards of half-molecule IgA proteins in the mouse (Potter and Kuff, 1964), many structural variants of both heavy and light chains have been recognized (see review by Franklin and Frangione, 1975). It seems likely that studies of these proteins will provide insights into the genetic control of immunoglobulins (Igs) which cannot be obtained from analyses of intact molecules. This report summarizes the clinical features of yand,t-heavy chain disease (HCD) and discusses some of the biochemical and biosynthetic studies which have clearly established that these abnormal proteins are products of disordered synthesis and not the result of degradation. In addition, several other structural abnormalities of heavy chains will be mentioned, excluding a-chain disease which is dealt with elsewhere. A detailed classification of the known alterations of heavy and light chains is given in a review by Franklin and Frangione (1975). Only alterations in man will be considered, although similar changes in heavy chains have recently been discovered in the mouse (Scharff, 1974; Milstein, Adetiegbo, Cowan, and Secher, 1974). In this article discussion will be limited to four major types: (1) heavy chain disease proteins; (2) myeloma proteins with altered heavy chains; (3) half-molecules; and (4) myelomas with degraded heavy chains.","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"6 ","pages":"65-71"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-6.1.65","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12015238","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":"Alpha-chain disease.","authors":"M Seligmann","doi":"10.1136/jcp.s1-6.1.72","DOIUrl":"https://doi.org/10.1136/jcp.s1-6.1.72","url":null,"abstract":"The pathological and clinical features of alpha-chain disease, its immunological diagnosis, the structural abnormalities of the abnormal immunoglobulin A compared with those of proteins of gamma and mu heavy chains diseases, the course of the disease and its present treatment, the epidemiological factors involved and their influence on pathogenesis and finally, the relationship with the \"Mediterranean abdominal lymphoma\" or IPSID are successively described. The stress has been placed on the latest data which refine but no not modify the first description of the disease. In the same way as studies on the synthesis and structure of proteins in heavy chain diseases will provide new data on the biosynthesis of normal immunoglobulins, so the elucidation of sequential events leading from a plasmocytic stage reversible by antibiotic therapy alone to a highly malignant immunoblastic stage should improve our knowledge of the genesis of human lymphomas.","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"6 ","pages":"72-6"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-6.1.72","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12015239","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":"Benign paraproteinaemias.","authors":"J Kohn","doi":"10.1136/jcp.s1-6.1.77","DOIUrl":"https://doi.org/10.1136/jcp.s1-6.1.77","url":null,"abstract":"A paraprotein can be defined in our present state of knowledge as a complete or incomplete immunoglobulin molecule, possibly abnormal, produced in excess by a single clone of immunocytes (Osserman and Fahey, 1968)","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"6 ","pages":"77-82"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-6.1.77","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11988819","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":"Activation of complement in relation to disease.","authors":"J M Versey, L Slater, J R Hobbs","doi":"10.1136/jcp.s1-6.1.38","DOIUrl":"https://doi.org/10.1136/jcp.s1-6.1.38","url":null,"abstract":"Activation of the complement system results in the sequential interaction of its protein constituents, producing a series of enzymes from their precursors, each of which acts on the next protein in the chain, forming interprotein complexes of two or more of the cleavage products. The consequences of such activation include increased vascular permeability, attraction of polymorphonuclear leucocytes, the enhancement of phagocytosis, and alterations in cell membranes resulting in lysis and death. The classical complement system involves nine components labelled Cl to C9 which react together in a manner described as a cascade (Macfarlane, 1964). Activation of the system is usually brought about by the combination of an antibody with an antigen, which activates the complement-binding site of the antibody molecule, thought to be situated on the CH2 domain. The antigen may be in solution or on a cell surface. The Cl molecule becomes attached first to the antibody through a specific component Clq (Muller-Eberhard, 1968), fixation of which allows alterations to occur in the rest of the Cl molecule, with the formation of an esterase CIS which is capable of activating later components. The full classical sequence in relation to haemolysis is shown in figure 1. Once activated, each component must become bound to its specific receptor, which may be either the previous component in the sequence or a nearby site on the red cell surface. The half-lives of these activated components can be very short indeed, of the order of milliseconds (Lachmann and Thompson, 1970). If the activated components fail to become bound they lose their binding sites and the capacity to activate later components in the sequence; they circulate in the plasma in their inactivated forms, which are of smaller molecular weight than their parent molecules, and are cleared from the circulation at varying rates. At many of the steps within the complement sequence small molecular weight products are formed with specific physiological functions. Activation of C3 is by far the most important. Increased vascular permeability is caused by the formation of a low molecular weight peptide C3a (Ward, 1969), together with the generation of a chemotactic agent 38 EA","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"6 ","pages":"38-44"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-6.1.38","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11990529","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":"Therapy of lipid disorders.","authors":"D M Krikler","doi":"10.1136/jcp.s1-5.1.72","DOIUrl":"https://doi.org/10.1136/jcp.s1-5.1.72","url":null,"abstract":"","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"5 ","pages":"72-7"},"PeriodicalIF":0.0,"publicationDate":"1973-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-5.1.72","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15681269","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":"Phospholipids and their metabolism.","authors":"D Gompertz","doi":"10.1136/jcp.s1-5.1.11","DOIUrl":"https://doi.org/10.1136/jcp.s1-5.1.11","url":null,"abstract":"Phospholipids are characterized by the presence of non-polar hydrophobic side chains and polar hydrophilic head groups. These chemical groupings make them particularly suitable compounds to serve as major constituents for biological interfaces","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"5 ","pages":"11-6"},"PeriodicalIF":0.0,"publicationDate":"1973-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-5.1.11","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15458936","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":"Lipid methodology.","authors":"D G Cramp","doi":"10.1136/jcp.s1-5.1.17","DOIUrl":"https://doi.org/10.1136/jcp.s1-5.1.17","url":null,"abstract":"Advances in our knowledge of the circulating lipids and lipoproteins have been dependent on developments in analytical methods. In the past decade or so important advances have been made in this field, and some of the techniques now available to the lipid biochemist include analytical ultracentrifugal flotation (Pedersen, 1945; Gofman, Lindgren, Jones, Lyon, and Strisower, 1951); preparative ultracentrifugation with subsequent chemical analysis of fractions (Lindgren, Elliott, and Gofman, 1951; Hillyard, Entenman, Feinberg, and Chaikoff, 1955; Havel, Eder, and Bragdon, 1955; Bragdon, Havel, and Boyle, 1956); complexing and precipitation with polyanions (Burstein and Samaille, 1960; Bernfeld, Donahue, and Berkowitz, 1957); electrophoresis using various media, including paper (Lees and Hatch, 1963), cellulose acetate (Margolis and Langdon, 1966), starch gel (Kunkel and Slater, 1952), polyacrylamide gel (Narayan, Narayan, and Kummerow, 1965), and agar and agarose gel (Scanu, Lewis, and Page, 1958; Uriel, 1964; Noble 1968); immunological techniques including immunoelectrophoresis (Grabar and Burtin, 1964) aind immunodiffusion (Mancini, Carbonara, and Heremans, 1965); membrane filtration (Stone and Thorp, 1966). Other physico-chemical methods such as gas-liquid chromatography (Woodford, 1964), nuclear magnetic resonance (Chapman and Morrison, 1966), refractometry (Lindgren and Nichols, 1960), electron microscopy, x-ray techniques (Palmer, Schmitt, and Chargaff, 1941), and infrared and circular dichroic spectroscopy (Scanu and Hirz, 1968) have their place in the research laboratory. However the two techniques most widely used have been ultracentrifugation with chemical analysis of the density-gradient fractions, and the various types of electrophoresis. Indeed it is on the basis of the latter techniques, with ultracentrifugation as the reference method, that the lipoprotein families have been characterized, thus enabling biochemists and clinicians to gain an understanding of their physiological and pathological significance. In most clinical laboratories, instead of quantita-","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"5 ","pages":"17-21"},"PeriodicalIF":0.0,"publicationDate":"1973-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-5.1.17","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15458937","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":"Cholesterol metabolism.","authors":"N B Myant","doi":"10.1136/jcp.s1-5.1.1","DOIUrl":"https://doi.org/10.1136/jcp.s1-5.1.1","url":null,"abstract":"the of cholesterol in","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"5 ","pages":"1-4"},"PeriodicalIF":0.0,"publicationDate":"1973-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-5.1.1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15458938","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":"Lipoprotein fractionation.","authors":"K Carlson","doi":"10.1136/jcp.s1-5.1.32","DOIUrl":"https://doi.org/10.1136/jcp.s1-5.1.32","url":null,"abstract":"Most of the methods used in the separation and fractionation of serum proteins have also been applied to the lipoproteins. Salt precipitationwas used as early as the last century to fractionate serum proteins, and with this technique a lipoprotein was isolated in fairly pure form for the first time by Macheboeuf (1929). The precipitation tcchniques most commonly used today are based on the precipitation of very-low-density and low-density lipoproteins by sulphated polysaccharides (Burstein and Samaille, 1955) (see below). Much of our preser't knowledge of the serum lipoproteins is based on the studies of Gofman and coworkers, who used a combination of analytical and preparative ultracentrifugation (DeLalla and Gofman, 1954). The analytical ultracentrifuge is not widely available but preparative ultracentrifugation which, in combination with lipid analysis of the separated fractions, remains one of the best tools for the study of serum lipoproteins, is quite widely used (Havel, Eder, and Bragdon, 1955; Furman, Howard, and Norcia, 1959; Hatch, 1968). Electrophoresis is one of the most important modern techniques for studying lipoproteins; an important milestone in its development, which led to the classification of hyperlipoproteinaemias of Fredrickson, Levy, and Lees (1967), was the inclusion of albumin in the buffer foi paper electrophoresis (Lees and Hatch, 1963). More recent techniques with agarose or cellulose acetate gel as supporting medium give better resolution of the lipoprotein pattern. Of other techniques, both ultrafiltration in combination with nephelometry and adsorption chromatography on glass powder or calcium phosphates have been used to a limited extent. Gel filtration techniques are fairly new and have mainly been used in the study of the apoproteins of the lipoproteins (Brown, Levy, and Fredrickson, 1970). Immunological methods such as immunoelectrophoresis and immunodiffusion have been invaluable in the study of the protein moiety of the lipoproteins. Such studies have been mainly qualitative (Hatch, 1968; Brown et al, 1970), but there are some quantitative studies (Lees, 1970). An excellent review of this field has been published by Hatch (1968). Practical Methods for Lipoprotein Fractionation","PeriodicalId":75995,"journal":{"name":"Journal of clinical pathology. Supplement (Association of Clinical Pathologists)","volume":"5 ","pages":"32-7"},"PeriodicalIF":0.0,"publicationDate":"1973-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1136/jcp.s1-5.1.32","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"15458940","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}