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S COHEN

Publications and source records attributed to S COHEN.

At least 19 recordsLinked to original sources

TEMPERATURE-SENSITIVE REPRESSION OF STAPHYLOCOCCAL PENICILLINASE.

In eight highly inducible strains of Staphylococcus aureus repression of the formation of penicillinase was temperature-sensitive under conditions suggesting direct thermal inactivation of the repressor. Restoration of repression required protein synthesis. These strains were resistant to benzylpenicillin and to many other antibiotics. One auxotrophic mutant had gredtly reduced temperature sensitivity but was still normally inducible. Six strains were relatively poorly inducible, exhibited a proportionately smaller increase in enzyme after exposure to elevated temperature, and were sensitive to antibiotics other than benzylpenicillin. Temperature sensitivity may be a useful character in studies of the physiology and genetics of the repression of staphylococcal penicillinase.

Anti-Bacterial Agents↗

PREPARATION AND PROPERTIES OF THE PEPTIDE CHAINS OF NORMAL HUMAN 19 S GAMMA-GLOBULIN (IGM).

1. A method is described for preparing pure samples of 19s gamma-globulin (IgM) from normal human serum by using successive steps of dialysis, density-gradient ultracentrifugation, chromatography on DEAE-cellulose, and gel filtration on Sephadex G-200. The yield of IgM (20-25mg./100ml. of serum) was equivalent to about one-quarter of that present in normal serum. 2. Analysis of the separated peptide chains of normal IgM and IgG (7s gamma-globulin) showed considerable differences in the amino acid composition of A chains from the two proteins; their respective B chains, on the other hand, were similar in composition. The carbohydrate of both proteins is confined almost entirely to the A chains; the IgM A chain contains about four times as much carbohydrate as the IgG A chain. 3. These findings support the view that the different classes of human immunoglobulin have B chains that are identical and A chains that are chemically distinct.

Amino Acids↗