About: Blood serum is a(n) research topic. Over the lifetime, 46843 publication(s) have been published within this topic receiving 993315 citation(s).
01 Feb 1949-Journal of Biological Chemistry
TL;DR: An investigation of the biochemical changes following experimental liver injury felt the need of a simple, rapid, and accurate method for determining the protein fractions in small amounts of serum and began with Kingsley’s biuret procedure.
Abstract: In the course of an investigation of the biochemical changes following experimental liver injury we felt the need of a simple, rapid, and accurate method for determining the protein fractions in small amounts of serum. Among the simpler procedures known, the biuret reaction seemed to offer the most encouraging possibilities. Variations and improvements in the application of the biuret reaction to clinical chemistry can be traced in the works of Autenrieth (l), Hiller (2), Fine (3), Kingsley (4), and Robinson and Hogden (5). Kingsley (6) simplified the technique by adding serum directly to a “one piece” reagent. Efforts have been made to increase the stability of such biuret reagents with ethylene glycol (7), tartrate (8), and citrate (9)) We began our investigation with Kingsley’s (6) method and report briefly on the two main difficulties encountered in its use. The first is that the total protein (TP) reagent and, to a lesser extent, the albumin (ALB) reagent are not sufficiently stable. The length of time they remain so depends upon the technique of their preparation. One consequence of this variable stability is a difficulty in duplicating calibration curves with different lots of reagent. Errors may arise when results with a new reagent are read from an old calibration curve. Serious errors occur if a reagent is used after the separation of any black deposit gives evidence of deterioration. A second difficulty has been that total protein estimations made with the TP reagent and read, as prescribed, from calibration curves prepared with the ALB reagent have tended to be too low. Recorded in Table I are the results of a number of analyses in which Kingsley’s biuret procedure has been compared with the Kjeldahl method2 on both normal and ab-
01 Sep 1955-Journal of Clinical Investigation
TL;DR: The relatively low density of the lipoproteins was utilized by Lindgren, Elliott, and Gofman to separate them from the other serum proteins by ultracentrifugal flotation, and quantitation was subsequently performed by refractometric methods in the analytical ultracentRifuge.
Abstract: In the past few years several methods have been developed for the analysis of serum lipoproteins Lindgren, Elliott, and Gofman (1) have utilized the relatively low density of the lipoproteins to separate them from the other serum proteins by ultracentrifugal flotation Quantitation was subsequently performed by refractometric methods in the analytical ultracentrifuge Separations of lipoproteins have also been made by Cohn fractionation in cold ethanol, and the quantities of lipoprotein have been estimated from the lipid content of the fractions (2, 3) Widely used at the present time is the method of zone electrophoresis with quantitation either by staining (4) or by chemical analysis of eluates from the support
20 Aug 1976-Science
TL;DR: Plasmodium falciparum can now be maintained in continuous culture in human erythrocytes incubated at 38 degrees C in RPMI 1640 medium with human serum under an atmosphere with 7 percent carbon dioxide and low oxygen.
Abstract: Plasmodium falciparum can now be maintained in continuous culture in human erythrocytes incubated at 38 degrees C in RPMI 1640 medium with human serum under an atmosphere with 7 percent carbon dioxide and low oxygen (1 or 5 percent). The original parasite material, derived from an infected Aotus trivirgatus monkey, was diluted more than 100 million times by the addition of human erythrocytes at 3- or 4-day intervals. The parasites continued to reproduce in their normal asexual cycle of approximately 48 hours but were no longer highly synchronous. The have remained infective to Aotus.
01 Jan 1963-
TL;DR: J.K. Kaneko, Serum Proteins and the Dysproteinemias, and M.H. Morris, The Vitamins.
Abstract: T.B. Farver, Concepts of Normality in Clinical Biochemistry. J.G. Hauge, DNA Technology in Diagnosis, Breeding, and Therapy. J.J. Kaneko, Carbohydrate Metabolism and Its Diseases. M.L. Bruss, Lipids and Ketones. J.J. Kaneko, Serum Proteins and the Dysproteinemias. L.J. Gershwin, Clinical Immunology. J.W. Harvey, The Erythrocyte: Physiology, Metabolism, and Biochemical Disorders. J.J. Kaneko, Porphyrins and the Porhyrias. J.E. Smith, Iron Metabolism and Its Disorders. W.J. Dodds, Hemostasis. J.G. Zinkl and M.B. Kabbur, Neutrophil Function. J.W. Kramer and W.E. Hoffmann, Clinical Enzymology. B.C. Tennant, Hepatic Function. D.F. Brobst, Pancreatic Function. W.E. Hornbuckle and B.C. Tennant, Gastrointestinal Function. G.H. Cardinet III, Skeletal Muscle Function. D.R. Finco, Kidney Function. G.P. Carlson, Fluid, Electrolyte, and Acid-Base Balance. J.A. Mol and A. Rijnberk, Pituitary Function. A. Rijnberk and J.A. Mol, Adrenocortical Function. J.J. Kaneko, Thyroid Function. L-E. Edqvist and M. Forsberg, Clinical Reproductive Endocrinology. T.J. Rosol and C.C. Capen, Calcium-Regulating Hormones and Diseases of Abnormal Mineral (Calcium, Phosphorus, Magnesium) Metabolism. R.B. Rucker and J.G. Morris, The Vitamins. M. Haskins and U. Giger, Lysosomal Storage Diseases. B.R. Madewell, Tumor Markers. C.S. Bailey and W. Vernau, Cerebrospinal Fluid. J.R. Turk and S.W. Casteel, Clinical Biochemistry in Toxicology. W.F. Loeb, Clinical Biochemistry of Laboratory Rodents and Rabbits. J.T. Lumeij, Avian Clinical Biochemistry. Appendixes. Index.
03 Feb 1997-Clinica Chimica Acta
TL;DR: The results by this method agree very well with those obtained by electrophoresis and salt fractionation and the method is simple, it has excellent precision and the reagents are stable.
Abstract: A rapid and reliable method for measuring serum albumin employing bromcresol green is described. The addition of albumin to a solution of bromcresol green in a 0.075 M succinate buffer pH 4.20 results in an increase in absorbance at 628 nm. The absorbance-concentration relationship is linear for samples containing up to 6 g/dl albumin. Bilirubin, moderate lipemia, and salicylate do not interfere with the analysis. The use of nonionic surfactant (Brij-35) reduces the absorbance of the blank, prevents turbidity and provides linearity. The results by this method agree very well with those obtained by electrophoresis and salt fractionation. The method is simple, it has excellent precision and the reagents are stable. A protein standard is introduced which can be employed for both the total serum proteins and albumin determinations.