Amino Acids and Serum Proteins. Advances in Chemistry Series, No. 44.

1965 ◽  
Vol 87 (5) ◽  
pp. 1152-1152
Author(s):  
Bernard S. Gould
Keyword(s):  
Amino Acids ◽  
Serum Proteins

scholarly journals THE BASIC AMINO ACIDS OF SERUM PROTEINS

1934 ◽  
Vol 104 (2) ◽  
pp. 347-350
Author(s):  
Richard J. Block ◽  
Daniel C. Darrow ◽  
M. Katherine Cary
Keyword(s):  
Amino Acids ◽  
Serum Proteins ◽  
Basic Amino Acids

222 Corn-expressed Phytase Modulates Serum Amino Acids and Proteomics Profiles in Nursery Pigs Fed with Low-protein, -calcium, and -phosphorous Diets

2021 ◽  
Vol 99 (Supplement_3) ◽  
pp. 116-116
Author(s):  
Cedrick N N Shili ◽  
Mohammad Habibi ◽  
Parniyan Goodarzi ◽  
Frank Kiyimba ◽  
Steve Hartsen ◽  
...  
Keyword(s):  
Amino Acids ◽  
Growth Performance ◽  
Growth Regulation ◽  
Serum Proteins ◽  
Bone Mineralization ◽  
Negative Control ◽  
Differentially Expressed ◽  
High Dose ◽  
Blood Proteins ◽  
Low Protein

Abstract Feeding pigs with very low-protein (VLP) and low-phosphorous (P) diets may be useful for decreasing the nutrients excretion to the environment; however, this practice negatively impacts the animals’ growth performance. A beneficial effect of corn-expressed phytase (CEP) on growth performance of pigs fed with VLP diets was shown by our group recently. Little is known whether this improvement is related with alterations in profile of blood proteins and amino acids (AA). The objective of this study was to investigate whether supplementation of VLP, low-calcium (Ca) and low-P diets with a CEP can influence the serum AA and proteomics profiles in pigs. Forty-eight weaned barrows were subjected into one of the following groups (n = 8/group) for 4 weeks: positive control (PC), negative control-reduced protein (NC), NC+low-dose CEP, i.e 2,000 FTU/kg (LD), NC+high-dose CEP, i.e. 4,000 FTU/kg (HD), LD with reduced Ca/P (LDR), and HD with reduced Ca/P (HDR). At week 4, blood samples were collected from all pigs. Compared to PC, NC reduced the serum leucine and phenylalanine concentrations; however, LD recovered their levels. Using trypsinolysis and mass spectrometry, 703 serum proteins were identified and quantified, wherein 25 were found to be differentially expressed among groups. Hierarchical clustering showed a clear separation in proteins identified among dietary groups. Compared to NC, 23 and 24 proteins were found to be differentially expressed in serum of LD and HD groups, respectively, with some important proteins in growth regulation such as SELENOP being upregulated and the IGFBP family being downregulated in these groups. A positive correlation was detected between growth and abundance of BGN, TLN1, PDLIM1 and COL1A2 that are involved in bone mineralization and muscle structure development. Thus, CEP improved the serum profile of some essential AA and affected the expression of proteins involved in regulation of growth in pigs fed with VLP diets.

Evolution of Serum Proteins and Amino Acids on Hemodialysis and after Kidney Transplantation

2015 ◽  
pp. 110-115
Author(s):  
J. Pascual ◽  
R. Marc�n ◽  
R. Martin del Rio ◽  
M. E. Rivera ◽  
M. T. Naya ◽  
...  
Keyword(s):  
Amino Acids ◽  
Kidney Transplantation ◽  
Serum Proteins

scholarly journals THE MECHANISM OF ANAPHYLACTIC SHOCK

1915 ◽  
Vol 22 (4) ◽  
pp. 401-417 ◽  
Author(s):  
James W. Jobling ◽  
William Petersen ◽  
A. A. Eggstein
Keyword(s):  
Amino Acids ◽  
Anaphylactic Shock ◽  
Serum Proteins ◽  
Progressive Increase ◽  
Acute Intoxication ◽  
Foreign Protein ◽  
Serum Lipase ◽  
Maximum Period ◽  
Specific Protease ◽  
Protease B

1. The serum ferments are practically unaltered by a primary injection of foreign protein. 2. During the course of sensitization the injection of the antigen is followed by the mobilization of a non-specific protease which increases in rapidity and intensity as the maximum period of sensitization is reached. 3. Acute shock is accompanied by: (a) The instantaneous mobilization of a large amount of non-specific protease; (b) a decrease in antiferment; (c) an increase in non-coagulable nitrogen of the serum; (d) an increase in amino-acids; (e) a primary decrease in serum proteoses. 4. Later there is a progressive increase in the non-coagulable nitrogen, in proteoses, and in serum lipase. 5. The acute intoxication is brought about by the cleavage of serum proteins (and proteoses) through the peptone stage by a non-specific protease. 6. The specific elements lie in the rapid, mobilization of this ferment and the colloidal serum changes which bring about the change in antiferment titer.

scholarly journals Pinocytosis and intracellular degradation of exogenous protein: modulation by amino acids.

1983 ◽  
Vol 96 (6) ◽  
pp. 1586-1591 ◽  
Author(s):  
J M Besterman ◽  
J A Airhart ◽  
R B Low ◽  
D E Rannels
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Free Amino Acids ◽  
Free Amino ◽  
De Novo ◽  
Serum Proteins ◽  
Fluid Phase ◽  
Cellular Protein ◽  
Intracellular Degradation ◽  
Exogenous Protein

Intracellular degradation of exogenous (serum) proteins provides a source of amino acids for cellular protein synthesis. Pinocytosis serves as the mechanism for delivering exogenous protein to the lysosomes, the major site of intracellular degradation of exogenous protein. To determine whether the availability of extracellular free amino acids altered pinocytic function, we incubated monolayers of pulmonary alveolar macrophages with the fluid-phase marker, [14C]sucrose, and we dissected the pinocytic process by kinetic analysis. Additionally, intracellular degradation of endogenous and exogenous protein was monitored by measuring phenylalanine released from the cell monolayers in the presence of cycloheximide. Results revealed that in response to a subphysiological level of essential amino acids or to amino acid deprivation, (a) the rate of fluid-phase pinocytosis increased in such a manner as to preferentially increase both delivery to and size of an intracellular compartment believed to be the lysosomes, (b) the degradation of exogenously supplied albumin increased, and (c) the fraction of phenylalanine derived from degradation of exogenous albumin and reutilized for de novo protein synthesis increased. Thus, modulation of the pinosome-lysosome pathway may represent a homeostatic mechanism sensitive to the availability of extracellular free amino acids.

scholarly journals AUTORADIOGRAPHIC ANALYSIS ON AGAR PLATES OF ANTIGENS FROM SUB CELLULAR FRACTIONS OF RAT LIVER SLICES

1961 ◽  
Vol 10 (3) ◽  
pp. 411-423 ◽  
Author(s):  
W. S. Morgan ◽  
P. Perlmann ◽  
T. Hultin
Keyword(s):  
Amino Acids ◽  
Rat Liver ◽  
Serum Proteins ◽  
Free Cell ◽  
Radioactive Material ◽  
Rat Serum ◽  
Agar Diffusion ◽  
Liver Slices ◽  
Ionic Detergent ◽  
Typical Cell

Slices of rat livers were incubated with 14C amino acids, homogenized, and subjected to differential centrifugation. The microsomes were further extracted with the non-ionic detergent Lubrol W and with EDTA. These extracts and the microsome free "cell sap," freed from the pH 5 precipitable fraction, were subsequently reacted with antisera using agar diffusion techniques. The antisera employed were obtained from rabbits injected with different subcellular fractions of rat liver or with rat serum proteins. When the agar diffusion plates were autoradiographed it was found that some of the precipitates were radioactive while others were not. Control experiments indicated that this labeling was due to the specific incorporation of 14C amino acids into various rat liver antigens during incubation of the slices rather than to a non-specific adsorption of radioactive material to the immunological precipitates. When the slices were incubated with the isotope for up to 30 minutes, the serum proteins which could be extracted from the microsomes with the detergent were strongly labeled, as were a number of additional microsomal antigens of unknown significance. In contrast, the serum proteins present in the cell sap were only weakly labeled. Most of the typical cell sap proteins, both those precipitable and those soluble at pH 5, seemed to remain unlabeled. No consistently reproducible results were obtained with the EDTA extracts of the ribosomal residues remaining after extraction of the microsomes with the detergent. Incubation of the liver slices for longer periods (up to 120 minutes) led to a strong labeling of the serum proteins in the cell sap as well as to the appearance of labeling in additional cell sap proteins. The results are discussed with regard to the subcellular site of synthesis and the metabolism of the different antigens.

Inhibition of Incorporation of S35-Labeled Amino Acids into Tissue and Serum Proteins by Beta-3-Thienyl-DL-alanite

1961 ◽  
Vol 109 (3) ◽  
pp. 223-230 ◽  
Author(s):  
A. Szentivaniyi ◽  
Z. Hruban ◽  
J. Radovich ◽  
D. W. Talmage
Keyword(s):  
Amino Acids ◽  
Serum Proteins

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 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.

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