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Biomedical subjects

H B Bosmann

Publications and source records attributed to H B Bosmann.

At least 91 records · Page 5Linked to original sources

Serum and host liver activities of glycosidases and sialyltransferases in animals bearing transplantable tumors.

Rats bearing Reuber H-35 or Novikoff hepatomas and mice bearing L1210 or L5178Y murine leukemias exhibited elevated serum levels of fetuin : N-acetylneuraminic acid transferase (EC 2.4.99.1) activity. The serum transferase activity could be correlated with the growth rate of the tumor; in animals bearing the more rapidly growing Novikoff hepatoma, activity was higher than in animals bearing the Reuber H-35 hepatoma. Higher transferase levels were also found in L1210 leukemic mice than in mice with the slightly slower growing L5178Y leukemia. Serum from rats bearing Reuber H-35 hepatoma and mice bearing L1210 murine leukemia had elevated levels of alpha- and beta-glucosidase (EC 3.2.1.20 and EC 3.2.1.21), alpha- and beta-galactosidase (EC 3.2.1.22 and (3.2.1.23), beta mannosidase (EC 3.2.1.25), alpha- and beta-fucosidase (EC 3.2.1.- and EC 3.2.1.38), beta-N-acetylglucosaminidase (EC 3.2.1.30) and acid phosphatase (EC 3.1.3.2); alpha-mannosidase (EC 3.2.1.24), beta-N-acetylgalactosaminidase (EC 3.2.2.-) and beta-xylosidase (EC 3.2.1.37) were not elevated. In animals bearing Reuber H-35 hepatoma, host liver levels of glycosidases, beta-glucuronidase (EC 3.2.1.31) and acid phosphatase were elevated over both the control and the hepatoma values. The data are interpreted to mean that the tumors or various host tissues release large quantities of enzymes into the serum and that enzyme levels in host organs may also be affected by the tumor.

Acid Phosphatase↗

Properties of rat cerebral cortex neuronal nuclear surfaces: electrokinetic parameters.

Rat cerebral cortex neuronal nuclei were isolated by a mild technique utilizing sucrose; citric acid was not used in the isolation of the nuclei. These nuclei in 0.0145 M NaC1, 4.5 per cent sorbitol, and 0.6 mM NaHCO3 with pH 7.2 plus or minus 0.1 at 25 degrees C had an electrophoretic morbidity of minus 2.01 mum-s(-1)-V(-1)-cm(-1). The mobility curves for the brain nuclei indicated that the surface had an acid-dissociable group of pK APPROXIMATELY 2.7. Nuclei treated with 50 mg neurominidase/mg particle protein had a mobility of minus 1.4 mum-s(-1)-V(-1)-cm(-1). DNase or RNase at 50 mug/mg protein had no effect on the mobility of the isolated nuclei. Concanavalin A at 50 mug/mg protein decreased the nuclei electrophoretic mobility to minus 1.82 mum-s(-1)-V(-1)-cm(-1). The results are interpreted to mean that the brain nuclear external surface contains terminal sialic acid residues, but it is completely devoid of nucleic acids, and it binds canavalin A.

Animals↗