scholarly journals The Lack of Selective Reincorporation into Tissue Protein of the Amino Acids Derived from the Catabolism of Serum Protein

1963 ◽  
Vol 47 (2) ◽  
pp. 297-314 ◽  
Author(s):  
Jevrosima Radovich ◽  
Andor Szentivanyi ◽  
David W. Talmage
Keyword(s):  
Amino Acids ◽  
Serum Protein ◽  
Gamma Globulin ◽  
Serum Proteins ◽  
Time Intervals ◽  
Time Activity ◽  
Beta Globulin ◽  
Specific Activities ◽  
Zero Time

Homologous S35-labeled albumin, gamma globulin, and alpha-beta globulin were transfused into rabbits and the specific activities of the electrophoretic fractions of the sera of the recipients were determined at various time intervals up to 12 days after injection. Detectable reincorporation into a fraction other than that transfused was found only in the gamma globulin fraction after albumin injection. This activity rose between 2 and 12 days and reached a level of 2 to 3 per cent of the extrapolated zero time activity of the albumin fraction. When homologous serum protein doubly labeled with I131 and S35 was transfused into mice, marked drops in the ratios of I131 to S35 in the serum and tissue proteins were observed between 1 and 48 hours after injection. On the basis of a determination of the absolute and relative amounts of I131 and S35 found in the various tissue and serum proteins, the amount of reincorporation of S35 into each protein was calculated. The relative amounts of reincorporation of S35 among the various tissues were remarkably similar to the relative amounts of incorporation of S35 after the injection of labeled free amino acids. It is concluded that serum protein does not form a major direct source of amino acids to the tissues but feeds them indirectly through the extracellular pool.

scholarly journals The Metabolism of Serum Proteins in Neonatal Rabbits

1960 ◽  
Vol 43 (6) ◽  
pp. 1047-1059 ◽  
Author(s):  
Maria P. Deichmiller ◽  
Frank J. Dixon
Keyword(s):  
Serum Protein ◽  
Half Life ◽  
Gamma Globulin ◽  
Serum Proteins ◽  
Growth Period ◽  
Unit Weight ◽  
Total Serum Protein ◽  
Total Serum ◽  
Beta Globulin ◽  
Newborn Animals

1. Incorporation of S35-labeled amino acids into serum proteins has been studied in neonatal and developing rabbits. It was found that, per unit weight, neonatal rabbits synthesized only about 1/36 of the gamma globulin, 1/7 of the beta globulin, ½ of the alpha globulin, and ⅛ of the albumin that an adult synthesized. The growing rabbit developed the ability to synthesize various serum proteins at different times. 2. Plasma volumes and serum protein concentrations were determined at different times during the growth period of the rabbit. Plasma volumes were found to be 1 and ½ times larger in newborn animals than in adults, with a gradual decline to the adult level. The total serum protein concentration at birth was about 60 to 65 per cent of the adult value and gradually increased with growth as the plasma volume decreased. 3. Half-lives of homologous albumin and gamma globulin were studied. The half-life of albumin in neonates was nearly twice as long as the half-life in adults, the latter value being reached at 1 month of age. The half-life of gamma globulin in neonates was more than twice as long as the half-life in adults and reached adult values at 2 to 3 months. 4. Attempts were made to alter serum protein metabolism. Gamma globulin synthesis early in life was augmented with antigen injections.

scholarly journals SITES OF FORMATION OF IMMUNE GLOBULINS AND OF A COMPONENT OF C'3

1961 ◽  
Vol 114 (4) ◽  
pp. 459-470 ◽  
Author(s):  
G. M. Hochwald ◽  
G. J. Thorbecke ◽  
R. Asofsky
Keyword(s):  
Amino Acids ◽  
Serum Protein ◽  
Liver Tissue ◽  
Serum Proteins ◽  
Mouse Serum ◽  
Spleen Tissue ◽  
Specificity And Sensitivity ◽  
Immune Globulins

The development of a new method for the determination of the sites of serum protein formation has been described. The method involves the incorporation of C14-labeled amino acids by tissues cultured in vitro, and subsequent autoradiography of immunoelectrophoretic patterns prepared from a mixture of culture fluids and carrier serum with an antiserum against the carrier serum. This technique has been used to demonstrate formation of γ-globulin, of ß2-macroglobulin, and of a component of C'3 by mouse spleen tissue, and of various other serum proteins by liver tissue. The specificity and sensitivity of this method have been discussed, and some of its advantages and pitfalls were mentioned. In addition, a rabbit antimouse serum was prepared, and the immunoelectrophoretic patterns obtained with mouse serum were compared with those described in the literature.

CHILDHOOD TUBERCULOSIS: CLINICAL VALUE OF THE ELECTROPHORETIC PATTERN OF THE SERUM PROTEINS

PEDIATRICS ◽  
1961 ◽  
Vol 27 (1) ◽  
pp. 54-67
Author(s):  
Rosa Lee Nemir ◽  
Charlotte Marker Zitrin ◽  
Paraskevi Tsouros ◽  
Enriqueta Melly
Keyword(s):  
Serum Protein ◽  
Tuberculous Meningitis ◽  
Gamma Globulin ◽  
Serum Proteins ◽  
Electrophoretic Pattern ◽  
Miliary Tuberculosis ◽  
Protein Fractions ◽  
Reciprocal Relation ◽  
Tuberculous Infection ◽  
Tuberculous Disease

The blood serum protein fractions of 138 children with tuberculosis were analyzed by paper electrophoresis serially over a period of many months. Many manifestations of tuberculous infection were studied. The group was divided into 11 categories ranging from healed or arrested tuberculous disease to various stages of activity. The serum protein fractions were evaluated in terms of prognosis, type of tuberculous disease, effect of intercurrent infection and age of patient. It was found that the greatest changes occurred in the gamma-globulin and albumin fractions in reciprocal relation. With the exception of tuberculous meningitis, the increase in gamma-globulin usually corresponded to the severity of disease. Albumin was correspondingly decreased, and was low even in tuberculous meningitis. Both fractions approached normal levels as the patients improved. Relatively normal readings were found in patients with tuberculosis observation or arrested tuberculosis. The greatest deviation from normal was seen in patients with miliary tuberculosis and those with pleurisy with effusion. Here, the gamma and alpha2-globulins were very high and the serum albumin was low. The alpha2 fraction was elevated in the children with more severe disease, including tuberculous meningitis; with clinical improvement it returned to normal more rapidly than the gamma. A rise in the beta-globulin fraction suggests caseation. Confirmatory evidence was obtained in patients with endobronchial disease, tuberculous adenitis and from the only necropsy in the series. The significant changes in the various fractions are further described and discussed.

PROTEIN TURNOVER IN WHEAT AND SNAPDRAGON LEAVES: PRELIMINARY INVESTIGATIONS

1963 ◽  
Vol 41 (7) ◽  
pp. 969-983 ◽  
Author(s):  
J. A. Hellebust ◽  
R. G. S. Bidwell
Keyword(s):  
Amino Acids ◽  
Protein Turnover ◽  
Soluble Sugars ◽  
Turnover Rates ◽  
Time Intervals ◽  
Protein Nitrogen ◽  
Protein Amino Acids ◽  
Specific Activities ◽  
Wheat Leaves ◽  
Biochemical Differentiation

Detached primary wheat leaves and attached cotyledons and primary leaves of snapdragons were allowed to photoassimilate C14O2 for short periods of time. They were subsequently kept in air and samples were taken at various time intervals and analyzed for protein nitrogen, and amounts and total radioactivities of soluble sugars and amino acids and protein amino acids. A method of estimating protein turnover from these data is discussed. Amounts and specific activities of respired carbon were also determined for wheat leaves.Minimum protein turnover rates of about 0.5 to 1.5% per hour were found in rapidly growing snapdragon leaves and in snapdragon cotyledons. Lower rates were found in detached, non-growing wheat leaves and slowly growing snapdragon leaves. Little contribution could have been made by proteins as substrates for respiration in detached wheat leaves. It is suggested that protein turnover in leaves is mainly associated with growth and biochemical differentiation.

Simplified Technic for the Determination of Serum Protein-Bound Iodine

1961 ◽  
Vol 7 (6) ◽  
pp. 637-645 ◽  
Author(s):  
Louise W Faulkner ◽  
Richard P Levy ◽  
Jack R Leonards
Keyword(s):  
Serum Protein ◽  
Sodium Carbonate ◽  
Room Temperature ◽  
Sodium Carbonate Solution ◽  
Serum Proteins ◽  
Internal Standard ◽  
Temperature Correction ◽  
Carbonate Solution ◽  
Correction Formula

Abstract A simplified technic for the determination of serum protein-bound iodine (PBI) is presented. Endogenously labeled l131 PBI is completely recovered. The technic is based on the method of Barker et al. (1) and includes the following modifications: The number of washes of the precipitated serum proteins are decreased. Unashed iodide standards are used in a sodium carbonate solution rather than an internal standard. A temperature-correction formula is employed to allow the cericarsenite-iodide reaction to be carried out at room temperature, and a stable cerate color is produced with brucine sulfate so that the colorimetry is carried out with greater convenience. The serum PBI concentrations are read directly from a graph, which simplifies the calculations.

scholarly journals KINETICS OF AMINO ACID INCORPORATION INTO SERUM PROTEINS

1955 ◽  
Vol 38 (3) ◽  
pp. 283-293 ◽  
Author(s):  
H. Green ◽  
H. S. Anker
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Serum Protein ◽  
Transit Time ◽  
Serum Proteins ◽  
Amino Acid Incorporation ◽  
Acid Incorporation ◽  
Amino Acid Analogues ◽  
Kinetics Of

1. The effect of varying body temperature on the rate of amino acid incorporation into serum protein does not give support to the idea that the rate of this process is adjusted in vivo to restore those protein molecules destroyed by thermal denaturation. The experimentally observed Q10 was about 3.9. 2. When amino acids are injected into the blood of animals in a steady state of serum protein turnover, a period of time elapses before these amino acids can be found in the serum proteins. This has been called transit time. At a given temperature (31°) it is the same in rabbits, turtles, and Limulus (1 hour). In rabbits and turtles it has a Q10 of 3.2. It appears to be specifically related to the process of synthesis (or release) of serum proteins. 3. It was not possible to affect the transit time or the incorporation rate by the administration of amino acid analogues.

An Evaluation of Serum Protein Fractionation Using a Methyl Orange Method for Determination of Albumin

1964 ◽  
Vol 10 (12) ◽  
pp. 1131-1136 ◽  
Author(s):  
Leonard V Crowley
Keyword(s):  
Methyl Orange ◽  
Serum Protein ◽  
Serum Proteins ◽  
Poor Correlation ◽  
Automated Systems ◽  
Protein Fractionation ◽  
Dye Binding

Abstract Fractionations of serum proteins using dye-binding methods have become popular because such methods are simple and can be adapted easily to automated systems of analysis, and the results of analysis performed on normal serums correlate well with results obtained by other methods. However, the good correlations do not necessarily apply when dealing with abnormal serums. Analysis of a selected group of serums revealed in 14% of cases a relatively poor correlation between fractionation by electrophoresis and a method involving dye binding. Methods of protein fractionation involving dye binding are satisfactory for routine use provided the limitations of these methods are recognized.

THE DETERMINATION OF SERUM PROTEIN FRACTIONS ON FILTER PAPER ELECTROPHEROGRAMS BY THE BIURET REACTION, AND SOME OBSERVATIONS ON THE SERUM PROTEINS OF THE ESTROGENIZED IMMATURE PULLET

1954 ◽  
Vol 32 (1) ◽  
pp. 189-199 ◽  
Author(s):  
W. P. McKinley ◽  
W. A. Maw ◽  
W. F. Oliver ◽  
R. H. Common
Keyword(s):  
Serum Protein ◽  
Filter Paper ◽  
Domestic Fowl ◽  
Serum Proteins ◽  
Paper Electrophoresis ◽  
Protein Fractions ◽  
Veronal Buffer

An application of the biuret reaction to the determination of protein fractions on filter paper electropherograms of serum is described. The relative mobilities of the serum protein fractions of the domestic fowl and of man are compared. Values are reported for serum protein fractions as separated by filter paper electrophoresis in a methanolic veronal buffer. Some observations on the serum proteins of the estrogenized immature pullet are reported; and it is tentatively suggested that another fraction as well as serum phosphoprotein appears in the serum of the pullet as a consequence of treatment with estrogen.

scholarly journals OPTIMIZATION OF PARAMETERS OF FERMENTOLYSIS OF PROTEINS IN THE COMPOSITION OF SERUM-PROTEIN CONCENTRATE

2019 ◽  
Vol 12 (4) ◽  
Author(s):  
N. Tkachenko ◽  
L. Lanzhenko ◽  
D. Skripnichenko ◽  
N. Kuprina ◽  
А. Hanicheva
Keyword(s):  
Amino Acids ◽  
Serum Protein ◽  
Free Amino Acids ◽  
Free Amino ◽  
Serum Proteins ◽  
Raw Material ◽  
Short Chain ◽  
Optimal Parameters ◽  
Cosmetic Products ◽  
Nanofiltration Concentrate

The food industry is a strategic industry that works quite steadily even during periods of economic crises, providing food security to any state, and is a source of raw material for other industries with a high potential for development, for example, for the production of cosmetics. The modern cosmetics market is represented by various cosmetic products, often expensive, but not always made from natural ingredients. Therefore, the search for the newest ingredients for the production of natural cosmetics on the basis of domestic raw materials is an urgent task of the present. Ingredients from milk serum can be used for the production of natural cosmetics that in large quantities is obtained in milk processing enterprises and often remains unprocessed. Whey protein concentrations can be a source of short-chain peptides and free amino acids for the production of various cosmetic products. The process of fermentolysis of serum proteins in nanofiltration concentrate KSB-65 with the content of dry matter of 20% using neutral peptidase C from the domestic producer at a temperature of 40 ºС with the duration of the process varying from 1 to 5 hours, the content of peptidase – from 0,5 to 2,0 U/g. It is established that the optimal parameters of the fermentolysis of serum proteins in KSB-65 are as follows: temperature 40 º C, neutral peptidase C content – 0.78 U/g, duration of fermentolysis – 3.17 hours. With optimal parameters of the fermentolysis process, the hydrolyzate of the nanofiltration concentrate KSB-65 contains the maximum amount of short chain peptides (57.03 mg/cm3) and a high concentration of free amino acids (54.66 μg/cm3). Recommendations for the further use of serum protein hydrolyzate obtained using the recommended optimal parameters of the enzyme production process from the nanofiltration concentrate KSB-65, in the manufacture of cosmetic products, including with anti-age effect, and hydrolyzates of proteins enriched with probiotic cultures of lactam bifidobacteria or their lysates.

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