Homologous Serum Albumin Research Articles

Immunological characterization of a diabetogenic protein from bovine adenohypophysis

1. 1. A diabetogenic protein isolated from bovine adenohypophysis which had previously been demonstrated to cause fasting hyperglycemia and decreased glucose tolerance in dogs and man is highly antigenic when injected into rabbits. 2. 2. Immunoelectrophoresis and gel double diffusion studies did not provide evidence of multiple antibodies or antigens in the bovine diabetogenic protein: anti-bovine diabetogenic system. 3. 3. Results of agar diffusion studies in which anti-bovine diabetogenic protein serum did not visibly react with homologous bovine serum proteins, serum albumin, ACTH or prolactin lend supporting evidence for the homogeneity of the reaction between bovine diabetogenic protein and its antiserum. 4. 4. A comparative immunological study of diabetogenic proteins from various species was performed using agar double diffusion studies.

In vitro catabolism of heterologous and homologous serum albumin by lysosomal enzymes.

SummaryThe products of hydrolysis and reaction rates for the degradation of homologous and heterologous serum albumin by lysosomal enzymes from spleen and liver were compared. The products of the degradation of homologous and heterologous serum albumin are similar with the exception of the small peptides with a mol wt less than 1000. A greater quantity of these small peptides were found in the degradation of heterologous serum albumin. Liver lysosomal enzymes hydrolyze heterologous serum albumin more rapidly and to a greater extent than homologous serum albumin.The ability of an animal to distinguish between native and foreign proteins may be dependent upon the proteolytic enzymes which catabolize such proteins. The greater degradation of foreign protein by liver suggests that mechanism for differentiation of homologous and heterologous protein may reside with lysosomal enzymes.

Immunologic characterization of a lung surfactant preparation.

Bovine lung surfactant was prepared from fresh lungs by homogenization, centrifugation in a high-density solution, and starch block electrophoresis. On injection into chickens, an antiserum was obt...

Elimination of Homologous And Heterologous (Bovine) Serum Albumin from the Blood Circulation in the Dog)

The elimination of intravenously administered I131-labelled bovine serum albumin has been compared to the elimination rate of relabelled homologous serum albumin in normal and bled dogs, which had lost considerable blood volumes. The investigation shows that during the first four to five days after the administration the elimination is similar of heterologous and homologous serum albumin. This proves that bovine serum albumin can be regarded to be an equivalent plasma expander to homologous serum albumin in the dog. Elimination of homologous as well as heterologous serum albumin follows a simple exponential curve during four to five days after administration. The intravascular half-lives for homologous serum albumin were 6.4 ±1.5 days and 6.4 ± 0.6 days respectively in control and bled dogs. Corresponding values for heterologous (bovine) serum albumin were 5.0 ± 0.3 and 4.8 ± 0.4 days respectively. The quote for cencentrations of homologous and heterologous serum albumin in different tissues was found to be relatively constant approximately 1.4. An exception was the stomach wall in bled dogs which had a quote of 1.1 only.

The intestinal absorption of pig and bovine immune lactoglobulin and human serum albumin by the new-born pig.

1. Homologous and heterologous colostral immune globulins and human serum albumin were fed to new-born pigs and an attempt was made to estimate the amounts appearing subsequently in serum.2. All three proteins, fed separately in large amounts to different pigs, appeared in the serum in low concentration about 45 min after feeding, and then rose quickly to a high level. No difference could be detected between the amounts absorbed when equal amounts had been fed but there was a wide variation between pigs. Previous dialysis of pig colostrum against bicarbonate saline did not affect the rate or amount of pig immune globulin absorbed after feeding.3. When pig and bovine colostral IgG were fed together at equal concentrations in bovine colostrum, the absorption of pig IgG was greater than that of bovine IgG. Human serum albumin, added to bovine colostral IgG in bovine colostrum, was absorbed readily and this did not interfere significantly with the absorption of bovine colostral IgG.4. The efficiency with which the pig intestine absorbed bovine colostral IgG depended on the dose and/or concentration fed, increasing as the dose fed was increased to 2 g and remaining constant for higher doses.5. Some of the absorbed immune globulin was shown to exist in a partly degraded form.6. The process of protein transfer across the intestine of the new-born pig may select, to a limited degree, between different proteins, but the digestion of protein shown to take place and the large variation between individual pigs makes interpretation of these results uncertain.

Albumin absorption by renal proximal tubule cells.

IT is widely accepted that different types of foreign proteins are absorbed by renal proximal tubule cells when present in the glomerular filtrate. Very little is known, however, about the way in which proximal tubules handle serum proteins, although these may be present in the proximal tubule fluid under both normal1,2 and pathological conditions. The present experiments were carried out to determine whether homologous serum albumin can be absorbed by proximal tubule cells and, if so, to determine by means of autoradiography at the electron microscopical level which cellular components participate in the absorption.

Local capillary permeability and exchangeable albumin in various organs of the rat

It was shown that the various organs and tissues differ from each other: (1) in the local capillary permeability for homologous I131-labeled serum albumin, and (2) in their contents of exchangeable albumin.

Half-lives of homologous serum albumins in several species.

SummaryThe half-lives of homologous serum albumins in humans, cows. dogs, rabbits and mice have been presented. The albumin half-lives are similar to the gamma globulin half-lives for the same species and apparently are dependent upon the metabolic characteristics of the host.

Antigenic Properties of Some Azo Compounds of Serum Albumin and Serum Globulin

Mulinos and Schlesinger have shown that when the proteins of egg white or of homologous blood serum are linked to antipyrine through an azo group, the resulting compounds are antigens capable of eliciting precipitins in rabbits and shock or uterine spasm in guinea pigs. The present report relates to similar experiments with analogous antigens prepared by coupling diazo compounds with homologous serum albumin and globulin. The results with the azo proteins from serum albumin were analogous to those obtained with whole serum, in that precipitative reactions were readily obtained and were inhibited by the preliminary addition of the original amino compounds employed for the preparation of the azo proteins. On the other hand, the azo derivatives of serum globulin failed to display antigenic character. The serum albumin and globulins, prepared in the usual manner by precipitation from saturated and half-saturated ammonium sulfate solution respectively, were coupled in weakly alkaline solution, according to the procedure of Landsteiner and Lampl, with the diazo compounds prepared from 4-amino antipyrine and anthranilic acid. After 2 hours at low temperature the mixture was acidified with acetic acid. The flocculent protein was repeatedly redissolved, then reprecipitated by acid, until the supernatant liquor remained colorless. The final azoprotein solutions were made up to contain 10 mg. of protein per cc. The effects of precipitins from rabbits upon the 4 types of azo protein are shown in Table I; inhibition by amino antipyrine and anthranilic acid is shown in Table II. The cases in which the azo groups showed antigenic reactions may be ascribed to the presence of serum albumin as a contaminant in the original globulin. It is of interest that the azo globulins were approximately twice as intensely colored as the azo albumins.