{"title":"Discriminant analysis.","authors":"H E Solberg","doi":"10.3109/10408367809150920","DOIUrl":"https://doi.org/10.3109/10408367809150920","url":null,"abstract":"<p><p>Discriminant analysis (DA) is a pattern recognition technique that has been widely applied in medical studies. It allows multivariate observations (\"patterns\" or points in multidimensional space) to be allocated to previously defined groups (diagnostic categories). The relationships between DA and other multivariate statistical techniques of interest in medical studies will be briefly discussed. The main emphasis is on linear discriminant functions (LDF). The theoretic assumptions underlying DA using LDFs will be presented, and the effect of violations to these assumptions will be reviewed in detail. Alternative methods will be presented when violations cause serious problems. It has been shown that the familiar LDF is fairly robust to departures from the assumptions. The application of the LDF in less than ideal situations therefore often does not cause much harm (if the violations are not too grotesque). Another set of problems reviewed is how to estimate the misallocation probabilities when using discriminant functions. The selection of the \"best\" subset of variables out of the complete set will be discussed. Practical guide lines are given based on the theoretic studies reviewed. When possible, available computer programs for various problems of DA will be indicated. The review does not aim at covering all medical studies where DA has been applied, since emphasis is on the practical conclusions of the theory of DA.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"9 3","pages":"209-42"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367809150920","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11608821","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":"Serum ferritin assay.","authors":"C P Alfrey","doi":"10.3109/10408367809150919","DOIUrl":"https://doi.org/10.3109/10408367809150919","url":null,"abstract":"<p><p>Ferritin is an iron storage protein of high-molecular weight which is primarily present in the liver, spleen, and bone marrow. A very sensitive immunoradiometric assay has been developed which permits determination of serum concentrations in normal persons and in patients with a variety of different disorders. In normal subjects, the serum ferritin concentration correlates very well with total body iron stores as measured by phlebotomy. The serum ferritin concentration is reduced in patients with iron-deficient anemia and is significantly higher in patients who are anemic for other reasons. Subject areas discussed in this review include the details of the immunoradiometric procedure, the sensitivity and accuracy of the assay, factors influencing the assay, values characteristic of a variety of clinical disorders, and the utility of the assay in clinical medicine and public health.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"9 3","pages":"179-208"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367809150919","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11608820","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":"Alteration of human serum ribonuclease activity in malignancy.","authors":"D Maor, M R Mardiney","doi":"10.3109/10408367909149733","DOIUrl":"https://doi.org/10.3109/10408367909149733","url":null,"abstract":"<p><p>A review of the literature and current biochemical studies is presented which provides significant evidence of alteration in the level of the enzyme ribonuclease activity in cancer. Current studies reveal that 80% of all cancer patients have alteration in ribonuclease activity and that individuals known to be at high risk for the development of cancer also demonstrate significant alteration of ribonuclease activity. It is noted that while elevation of serum ribonuclease exists within the cancer state and appears to be independent of clinical status (relapse, remission, or cured), diminished activity is found within the tumor itself. Animal models are reviewed which demonstrate that ribonuclease activity becomes elevated in the murine species subsequent to the transplantation of tumor and following the infection of the host with oncogenic virus. The occurrence of elevated ribonuclease activity in high tumor incidence strain mice long before the development of overt tumor is alos discussed. To date it is not possible to assign a specific function to the changes in the level of ribonuclease in connection with the cancer state. However, evidence indicating that tumor chemotherapy is generally associated with early elevation of ribonuclease activity within the tumor cell suggests that increased ribonuclease activity may play a role in the process by which the host restricts neoplastic transformation. The potential of this enzyme as a biochemical marker in cancer is discussed.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"10 1","pages":"89-111"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367909149733","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11953159","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 microbiology of paranasal sinus infections: diagnosis and management.","authors":"D H Rice","doi":"10.3109/10408367809150917","DOIUrl":"https://doi.org/10.3109/10408367809150917","url":null,"abstract":"<p><p>Study of the bacteriology of sinusitis and its diagnosis and treatment has been difficult. One problem is the anatomy of the paranasal sinuses; all communicate with a bacteriologically contaminated cavity. Access to all but the frontal sinus involves traversing either the nasal or oral cavity, both of which are teeming with aerobic and anaerobic bacteria. The criteria used to establish the diagnosis of sinusitis has varied widely. There are a number of examination techniques available, but none are foolproof. Therefore, patient populations may not be comparable. The absolute elimination of the possibility of contamination of culture specimens is impossible. Investigators have taken cultures in several ways: of the purulent secretions within the nose, of the contents lavaged from the sinus into the nose, of material aspirated from the sinus, and of tissue removed from the sinus. In most studies prior to 1974, anaerobic cultures were not performed. Studies of various treatment programs have used differing criteria to monitor the progress of treatment. No single method is completely reliable. Clinical signs and symptoms, radiologic appearance, the results of irrigation, and thermography have been used to follow patients. Many studies have used multiple therapeutic maneuvers concurrently, for example, antibiotics, lavage, and a decongestant. In some there were no controls. Because of these problems, as is true in many clinical areas of investigation, meaningful comparisons of various studies are difficult. Despite this, there are some areas of consensus in the literature.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"9 2","pages":"105-21"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367809150917","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11608817","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":"Clinical enzymology in cancer.","authors":"S F Markel","doi":"10.3109/10408367809150916","DOIUrl":"https://doi.org/10.3109/10408367809150916","url":null,"abstract":"<p><p>It is fair to say that so far, and with few exceptions, the application of enzymology to clinical oncology has been disappointing. This is certainly true with regard to cancer screening and diagnosis. It is unlikely that any single enzyme or isoenzyme will emerge as a sufficiently sensitive or specific indicator of cancer, and it would seem more profitable to focus on multivariate or pattern analysis of several enzymes and other measurable body fluid constituents. Another suggested approach would be to establish the normal enzyme levels for individuals and then follow them for changes which might signal the development of a neoplasm. Finally, Weber's concept of key enzymes as the phenotypic markers of neoplasia and targets of chemotherapy would appear to open a new avenue for enzymology in clinical oncology.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"9 2","pages":"85-104"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367809150916","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11608819","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":"Enzyme multiplied immunoassay technique: a review.","authors":"E G Curtis, J A Patel","doi":"10.3109/10408367809150923","DOIUrl":"https://doi.org/10.3109/10408367809150923","url":null,"abstract":"<p><p>A brief review of the various immunoassays is presented before the basic mechanism of the enzyme multiplied immunoassay technique (EMIT) is described. This is followed by a presentation of the specific advantages and disadvantages of this method, as well as its correlation with other methods as applied to qualitative and quantitative determinations of each type of drug for which EMIT technology is available.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"9 4","pages":"303-20"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367809150923","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11607682","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":"Newer aspects of pernicious anemia.","authors":"L Kass","doi":"10.3109/10408367809150914","DOIUrl":"https://doi.org/10.3109/10408367809150914","url":null,"abstract":"<p><p>Although readily treatable with vitamin B12, pernicious anemia continues to captivate investigative endeavors of those interested in the pathophysiology and pathogenesis of this disorder. Notable advances have been made in understanding properties of intrinsic factor, vitamin B12-binding proteins, structure and de novo synthesis of vitamin B12, mechanism of action of vitamin B12-dependent enzymes in man, and metabolic consequences of reduced activities of these enzymes in pernicious anemia. Similarly, newer morphological observations have given information regarding pathogenesis of some of the cytological abnormalities found in megaloblasts, and recent cytochemical studies have shed light on abnormalities of nuclear and cytoplasmic constituents in vitamin B12-deficient cells. Both cellular and humoral factors may contribute to immune-mediated processes in pernicious anemia, although as yet, it has not been established with certainty that pernicious anemia is an autoimmune disorder. As we look ahead, it will be important to define the process or processes responsible for atrophic gastritis, which is the pathophysiological basis of pernicious anemia. Likewise, advances in biophysics used in the study of cell membranes, cell surface phenomena, and metallic ion transport may find applicability in the study of pernicious anemia and perhaps provide further insights into metabolic abnormalities responsible for the development of megaloblastosis.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"9 1","pages":"1-47"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367809150914","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11607900","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":"Current considerations in digoxin usage.","authors":"W Shapiro","doi":"10.3109/10408367809150924","DOIUrl":"https://doi.org/10.3109/10408367809150924","url":null,"abstract":"<p><p>Basic considerations in biotransformation and pharmacodynamics are presented as a basis for understanding clinical usage. The role of polarity in determining a given glycoside's duration of action and extent of biotransformation is emphasized. The pharmacokinetics are summarized emphasizing the fact that digoxin is not completely absorbed by oral administration. The important relationship of serum digoxin levels to myocardial content and apparently to myocardial response is reviewed. This relationship and the development of precise methods for measurement of digoxin in serum provide the clinician with accurate means to assess myocardial tolerance for digoxin under diverse clinical circumstances. This review includes discussion of methods of digitalization, appropriate use of serum levels, apparent and real resistance to digoxin, and apparent and real sensitivity to digoxin. The limitations of serum levels as a precise guide to toxicity are analyzed. Finally, new developments in use of immunologic therapy for digoxin intoxication are presented.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"9 4","pages":"321-46"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367809150924","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11607683","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":"Methods for detection of hemoglobin variants and hemoglobinopathies in the routine clinical laboratory.","authors":"R G Schneider","doi":"10.3109/10408367809150921","DOIUrl":"https://doi.org/10.3109/10408367809150921","url":null,"abstract":"<p><p>Many mutant hemoglobins and hemoglobinopathies can be identified with a high degree of specificity in the routine clinical laboratory. The most frequent abnormalities--those involving Hb S or C--are usually easily detectable in small amounts of sample analyzed by two simple methods of electrophoresis: cellulose acetate at pH 8.5 and citrate agar at pH 6. Some rarer mutants, e.g., Hb O, Hope, and Camden, can also be recognized by these two methods. Presumptive identification of other relatively frequent mutants, such as Hb D Los Angeles (Punjab) and Hb G Philadelphia, can be accomplished with additional data obtained from globin electrophoresis on cellulose acetate in acidic and alkaline buffers containing urea and 2-mercaptoethanol (or dithioerythritol). Electrophoretic profiles are presented of about a dozen hemoglobins likely to be encountered in screening programs in the U.S. Methods are also presented for identifying other genetic hemoglobin abnormalities--various types of thalassemia, Hb M, unstable hemoglobins, and those of the newborn.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"9 3","pages":"243-71"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367809150921","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11608822","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 value of the amylase/creatinine clearance ratio in the diagnosis of acute pancreatitis.","authors":"A R Solomon","doi":"10.3109/10408367809150926","DOIUrl":"https://doi.org/10.3109/10408367809150926","url":null,"abstract":"<p><p>Acute pancreatitis usually confronts the clinician with a difficult diagnostic task. For years, the primary laboratory diagnostic tests were the serum and urine amylase and the serum lipase determinations. Recent studies have introduced the concept of the amylase/creatinine clearance ratio as a means of increasing the specificity of the laboratory diagnosis. This paper reviews the laboratory evaluation of acute pancreatitis with emphasis on the rationale, derivation, and specificity of the amylase/creatinine clearance ratio.</p>","PeriodicalId":75746,"journal":{"name":"CRC critical reviews in clinical laboratory sciences","volume":"9 4","pages":"367-80"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10408367809150926","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11316134","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}