CRC critical reviews in clinical laboratory sciences最新文献

{"title":"Plasma protein patterns in health and disease.","authors":"L M Killingsworth","doi":"10.3109/10408367909105852","DOIUrl":"https://doi.org/10.3109/10408367909105852","url":null,"abstract":"<p><p>The complex nature of protein metabolism has made interpretation of serum protein data a difficult task. Interpretive efforts can be facilitated by use of protein profiles which consist of quantitative immunochemical data combined with qualitative electrophoretic patterns. These profiles can be designed to clarify physiological relationships and emphasize pathological conditions through pattern recognition. This review will present protein profiles observed in acute, subacute, and chronic inflammation: liver diseases, protein losing disorders, plasma cell dyscrasias, humoral immune deficiencies, autoimmune diseases, genetic deficiency states, and other disorders. The value of consultative interaction and the use of combined profiles in the assessment of a patient's protein status will be covered. A discussion of protein patterns in normal individuals will include data on day-to-day, age- and sex-related variation. A section on management of protein data will present various approaches to profile reporting. Graphical report formats which minimize the time required for information transfer and simplify assimilation of results will be emphasized.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"11 1","pages":"1-30"},"PeriodicalIF":0.0,"publicationDate":"1979-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367909105852","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11596365","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Lipoprotein-X.","authors":"S Narayanan","doi":"10.3109/10408367909105853","DOIUrl":"https://doi.org/10.3109/10408367909105853","url":null,"abstract":"<p><p>Lipoprotein-X is an abnormal lipoprotein that appears in the sera of patients with obstructive jaundice, and thus is a sensitive indicator of cholestasis. In patients with familial plasma lecithin, Cholesterol acyltransferase (LCAT) deficiency, there is an inverse relationship between plasma Lp-X levels and LCAT activity. Ultracentrifugation procedures utilized for isolation of Lp-X have shown that it is associated with the low density lipoprotein fraction. Lp-X can be visualized by electrophoresis on either Agar or Agarose. The purity of Lp-X preparations has been documented by immunochemical procedures. The availability of highly purified antisera to Lp-X has served as a basis of one of the assay procedures for this lipoprotein. It's chemical composition has been established. Phospholipids and unesterified cholesterol constitute the bulk of the Lp-X molecule. Electron microscopic studies have demonstrated that Lp-X is a spherical particle which has strong aggregating properties. Membrane bound enzymes have been shown to aggregate with Lp-X. The fact that bile lipoprotein can be converted to Lp-X by the addition of albumin and that Lp-X can be converted to bile lipoprotein by the addition of bile salts offers a possible explanation for the origins of Lp-X. Phospholipases of plasma might play a role in the catabolism of Lp-X. The value and limitations of Lp-X determinations will also be addressed in this review.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"11 1","pages":"31-51"},"PeriodicalIF":0.0,"publicationDate":"1979-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367909105853","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11596366","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Selective ion monitoring in clinical chemistry.","authors":"I Björkhem","doi":"10.3109/10408367909105854","DOIUrl":"https://doi.org/10.3109/10408367909105854","url":null,"abstract":"<p><p>The principles of selective ion monitoring are described. Choice of instrumentations, derivatives, and internal standards is discussed. The most important factors influencing sensitivity, specificity, and precision are summarized. Applications of selective ion monitoring for quantitative assay of steroids, fat soluble vitamins, triglycerides, prostaglandins, biogenic amines, amino acids, carbohydrates, and several other organic compounds of clinical interest are critically reviewed. It is concluded that isotope dilution selective ion monitoring is one of the most sensitive and accurate techniques presently available for quantitation of a large number of endogenous compounds of clinical interest. In view of the high accuracy, the technique is useful not only for the clinical chemists dealing with determination of specific compounds which are difficult to analyze by other methods, but also for those dealing with quality control of routine analyses of simple organic compounds.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"11 1","pages":"53-105"},"PeriodicalIF":0.0,"publicationDate":"1979-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367909105854","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11444055","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Prophylaxis and therapy of venous thromboembolism.","authors":"A G Turpie,&nbsp;J Hirsh","doi":"10.3109/10408367909147136","DOIUrl":"https://doi.org/10.3109/10408367909147136","url":null,"abstract":"<p><p>Heparin is an anticoagulant drug which is used for the prophylaxis and treatment of venous thromboembolism and for the treatment of some cases of arterial thromboembolism. Venous thromboembolism is the commonest preventable cause of death in hospitalized patients, and the best approach to reduce its morbidity and mortality is the use of safe, effective, prophylaxis in patients at high risk. The use of low doses of heparin given s.c. (5000 units, 8 hourly)) has been shown in prospective clinical trials to be effective prophylaxis against venous thrombosis and nonfatal and fatal pulmonary embolism in patients undergoing general abdominothoracic surgery, without producing dangerous bleeding. Low-dose heparin, however, is not totally effective in patients undergoing hip surgery and suprapubic prostatectomy. The lack of benefit in these patients may be related to the intensity of the provocation to thrombosis. The use of heparin in large doses to treat thrombosis is associated with hemorrhagic complications in up to 30% of patients. There is evidence that continuous i.v. heparin is associated with fewer hemorrhagic complications than intermittent i.v. heparin, but the frequency is not related to the dose or to the use of laboratory monitoring. Hemorrhagic complications occur more frequently in elderly patients and in females and is more common following surgical operations. The frequency of recurrent venous thromboembolism is low in patients on therapeutic doses of heparin, and there is no difference in the frequency of recurrence in patients receiving heparin by continuous i.v. or intermittent i.v. administration.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"10 3","pages":"247-74"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367909147136","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11589875","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"New aspects of preleukemic disorders.","authors":"L Kass","doi":"10.3109/10408367909147138","DOIUrl":"https://doi.org/10.3109/10408367909147138","url":null,"abstract":"<p><p>Preleukemic disorders are a controversial group of panmyelopathic disturbances that often precede the emergence of acute myeloblastic or myelomonocytic leukemia. In most instances, these preleukemic disorders are characterized by slowly developing myeloblastosis of the bone marrow. They include preleukemia, primary acquired panmyelopathy with myeloblastosis or smouldering acute leukemia, erythroleukemia, and subacute myelomonocytic leukemia. Sometimes, transitions between these various preleukemic disorders may be observed in a single individual. Abnormalities in cellular differentiation are expressed in cytochemical aberrations and in elaboration of colony forming units by marrow cells of patients with preleukemic disorders. Cytogenic and cellular kinetic abnormalities link preleukemic disorders closely to acute myeloblastic or myelomonocytic leukemia, although in many patients with preleukemic disorders, conversion to acute leukemia is not observed or perhaps not recognized. Understanding pathogenetic and pathophysiological aspects of preleukemic disorders may shed light on aspects of cellular proliferation and cellular differentiation in the acute leukemias.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"10 4","pages":"329-96"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367909147138","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11505085","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cytochemistry of esterases.","authors":"L Kass","doi":"10.3109/10408367909147134","DOIUrl":"https://doi.org/10.3109/10408367909147134","url":null,"abstract":"<p><p>Esterases are enzymes that cleave aliphatic and aromatic ester bonds. With the use of synthetic substrates, esterases can be demonstrated in hematopoietic cells. Using alpha naphthyl acetate or alpha naphthyl butyrate, nonspecific esterase activity can be demonstrated. Intense activity of nonspecific esterase that is inhibited by fluoride is characteristic of cells of monocytic or reticulum cell origin. Using naphthol ASD-chloroacetate, specific esterase activity can be detected. Specific esterase is a lysosomal enzyme and is a useful marker for cells of granulocytic origin. Distinctive patterns of specific and nonspecific esterase activities are found in marrow cells from patients with various types of hematologic disorders. With the use of electrophoretic techniques, isoenzymatic analysis of esterases can be achieved.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"10 2","pages":"205-23"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367909147134","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11436623","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The hypercoagulability states.","authors":"C F Arkin,&nbsp;A S Hartman","doi":"10.3109/10408367909147139","DOIUrl":"https://doi.org/10.3109/10408367909147139","url":null,"abstract":"<p><p>Although interest in coagulation has usually centered about the various hemorraghic disorders, it is hyperactivity of the hemostatic system with its thrombotic complications which has a far greater clinical impact. The hypercoagulability states are a vague group of disorders not well defined by the laboratory. They fall into two distinct groups: (1) conditions promoting venous thrombosis by activating the coagulation mechanism and (2) conditions promoting arterial thrombosis by platelet plug formation. Dealing with both of these groups separately the various disorders associated with a hypercoagulable state are discussed as well as their pathophysiologic basis; Special emphasis is placed on the laboratory evaluation of these disorders.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"10 4","pages":"397-429"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367909147139","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11692596","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Leukapheresis and granulocyte transfusion.","authors":"J McCullough","doi":"10.3109/10408367909147137","DOIUrl":"https://doi.org/10.3109/10408367909147137","url":null,"abstract":"Granulocyte transfusion is becoming widely used in the treatment of infections in granulocytopenic patients. Several techniques are available for granulocyte collection. Some involve centrifugation of the whole blood and one removes granulocytes from whole blood by reversible adhesion to nylon fibers. The risks to the donor from leukapheresis do not appear to be greater than from whole blood donation. Granulocytes collected by centrifuge techniques function normally in vitro and have normal intravascular recovery and disappearance following transfusion. Granulocytes collected by filtration leukapheresis function almost normally in vitro but have a reduced intravascular recovery and abnormal kinetics as they leave the circulation. The role of leukocyte typing and compatibility testing for granulocyte transfusion is controversial. When the recipient has circulating antibody against donor leukocytes, transfused leukocytes do not circulate or migrate to sites of infection but are sequestered in the liver and spleen. Clinical studies have not defined whether patients benefit equally well clinically from transfusion of compatible or incompatible granulocytes. Initial reports of clinical trials of granulocyte transfusion were promising. However, similar patients who did not receive granulocytes were not studied. Most subsequent controlled trials showed a clear benefit from granulocyte transfusion while others did not. Differences in antibiotic therapy, chemotherapy, use of laminar flow rooms, and grouping of patients make it difficult to compare these clinical trials. Some, but not all, infected granulocytopenic patients benefit from transfusion. Granulocyte transfusions improve survival of granulocytopenic patients with gram negative sepsis and prolonged bone marrow aplasia. Studies are now attempting to identify other patients who should receive granulocytes, the optimum dose and schedule of transfusions, the optimum time to begin transfusion, and the value, if any, of prophylactic transfusions.","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"10 3","pages":"275-327"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367909147137","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11261189","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"2,3-Diphosphoglycerate: its role in health and disease.","authors":"R Juel","doi":"10.3109/10408367909147131","DOIUrl":"https://doi.org/10.3109/10408367909147131","url":null,"abstract":"<p><p>2,3-Diphosphoglycerate (2,3-DPG) was first discovered and isolated in 1925. However, it was not until 1967 that the function of 2,3-DPG was explained. This resulted in multiple research projects devoted to elucidating the mechanism by which 2,3-DPG exerts it effect on the oxygen affinity of hemoglobin. In addition, a vast amount of research has been devoted to assessing the role of 2,3-DPG in oxygen transport in various physiological and pathophysiological states. In many instances, the results of this research have produced conflicting data which have dampened the initial enthusiasm which followed the discovery of the function of 2,3-DPG. However, much of this conflicting data can be explained by the fact that 2,3-DPG is only one of a number of factors influencing the transport of oxygen to the tissues. Several of these factors influence oxygen transport independently as well as by altering the synthesis of 2,3-DPG and modifying its effect on hemoglobin. In spite of the conflicting results, the overall data gathered thus far appears to be sound enough to warrant the extensive research now being done, particularly in the area of blood storage and transfusion therapy.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"10 2","pages":"113-46"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367909147131","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11587085","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"beta 2-Microglobulin: methods and clinical applications.","authors":"M D Poulik,&nbsp;P Gold,&nbsp;J Shuster","doi":"10.3109/10408367909147135","DOIUrl":"https://doi.org/10.3109/10408367909147135","url":null,"abstract":"<p><p>beta 2-Microglobulin is a low molecular weight protein that is found in most biological fluids. It was originally isolated from urine of cadmium-poisoned patients. Its amino acid sequence was established and shown to be structurally related to immunoglobulin constant domains. With the aid of antibodies specific against beta 2-microglobulin, the protein was detected on the membranes of all nucleated cells, normal and neoplastic. Measuring the quantity of beta 2-microglobulin showed that high levels are present in patients with renal tubular deficiencies and several other pathological conditions including neoplastic diseases. Extremely high levels were detected in seminal fluid and colostrum. Despite the structural relationship to immunoglobulins, no immunological relationship was demonstrated with these proteins using antibodies specific for beta 2-microglobulin. However, such antibodies are cytotoxic to all cells carrying beta 2-microglobulin on their surfaces. The discovery that beta 2-microglobulin is an integral part of the histocompatibility antigens of human and murine origin stimulated further research and interest in this molecule. Several groups of investigators have shown that beta 2-microglobulin is the low molecular weight chain and is noncovalently bound to a high molecular weight chain which carries the histocompatibility antigens. The structure of the histocompatibility antigens of lymphocytes (HLA) was shown by immunochemical as well as biological methods, and it is now well accepted. The antibodies against beta 2-microglobulin are extremely useful in the isolation of the histocompatibility antigens for sequence studies. Furthermore, the antibody to beta 2-microglobulin revealed that other structures may be bound to beta 2-microglobulin such as phytohemoagglutimin (PHA) receptors, mixed lymphocyte culture (MLC) antigens, etc. Murine thymus leukemia (TL) antigen also contains beta 2-microglobulin as an integral part of its structure; other tumor antigens may have a similar structure. Through all these studies, beta 2-microglobulin emerged as the best known membrane protein that can serve as a model for study of the arrangement and the function of the cell membrane.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"10 3","pages":"225-45"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367909147135","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11309744","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}