Search PubMed⌕ Search

Biomedical subjects

H B Bosmann

Publications and source records attributed to H B Bosmann.

At least 109 records · Page 6Linked to original sources
PubMed1974

Enzyme activity in invasive tumors of human breast and colon.

Elevated levels of glycoprotein:sialyltransferase activity (EC 2.4.99.1; CMP-N-acetylneuraminate: D-galactosyl-glycoprotein N-acetylneuraminyltransferase) were found in human malignant neoplastic tissues compared to normal, benign, and "preneoplastic" tissues. This increase was not due to the cell density of the tissue. Elevated levels of certain proteases and glycosidases were also found. The increase in transferase activity may be associated with altered membrane synthesis in the neoplastic state; changes in the activity of degradative enzymes may be associated with tumor invasiveness and maintenance of the neoplastic state. Measurements on human tumors are possibly more directly relevant to cancer than those described for transformed fibroblastic cells in vitro.

Acid Phosphatase↗
PubMed1974

The lysosome periphery: biochemical and electrokinetic properties of the tritosome surface.

Normal rat liver lysosomes were isolated by the technique of loading with Triton WR-1339. Purity of the preparation was monitored with marker enzymes; a high enrichment in acid hydrolases was obtained in the tritosome fraction. In 0.0145 M NaCl, 4.5% sorbitol, 0.6 mM NaHCO(3), pH 7.2 at 25 degrees C the tritosomes had an electrophoretic mobility of -1.77 +/- 0.02 microm/s/V/cm, a zeta potential of 23.2 mV, a surface charge of 1970 esu/cm(2), and 33,000 electrons per particle surface assuming a tritosome diameter of 5 x 10(-7) m. Treatment of the tritosomes with 50 microg neuraminidase/mg tritosome protein lowered the electrophoretic mobility of the tritosome to -1.23 +/- 0.02 microm/s/V/cm under the same conditions and caused the release of 2.01 microg sialic acid/mg tritosome protein. Treatment of the tritosomes with hyaluronidase did not affect their electrophoretic mobility, while trypsin treatment elevated the net negative electrophoretic mobility of the tritosomes. Tritosome electrophoretic mobilities indicated a homogeneous tritosome population and varied greatly with ionic strength of the suspending media. pH vs. electrophoretic mobility curves indicated the tritosome periphery to contain an acid-dissociable group which likely represents the carboxyl group of N-acetylneuraminic acid; this was not conclusively proven, however, since the tritosomes lysed below a pH of 4 in the present system. Total tritosome carbohydrate (anthrone-positive material as glucose equivalents) was 0.19 mg/mg tritosome protein while total sialic acid was 3.8 microg (11.4 nmol)/mg tritosome protein. A tritosome "membrane" fraction was prepared by osmotic shock, homogenization, and sedimentation. Approximately 25% of the total tritosome protein was present in this fraction. Analysis by gas-liquid chromatography and amino acid analyzer showed the following carbohydrate composition of the tritosome membrane fraction (in microgram per milligram tritosome membrane protein): N-acetylneuraminic acid, 14.8 +/- 3; glucosamine, 24 +/- 3; galactosamine, 10 +/- 2; glucose, 21 +/- 2; galactose, 26 +/- 2; mannose, 31 +/- 5; fucose, 7 +/- 1; xylose, 0; and arabinose, 0. The results indicate that the tritosome periphery is characterized by external terminal sialic acid residues and an extensive complement of glycoconjugates. Essentially all the tritosome N-acetylneuraminic acid is located in the membrane and about 53% of it is neuraminidase susceptible.

Animals↗
PubMed1973

Electrokinetic properties of isolated cerebral-cortex synaptic vesicles.

Synaptic vesicles isolated from guinea-pig cerebral cortex had an electrophoretic mobility of -3.55mum.s(-1).V(-1).cm in saline-sorbitol, pH7.2, at 25 degrees C (ionic strength 0.015g-ions/1). The mobility was pH-dependent, varied with ionic strength and indicated that the vesicular surface contained weak acidic functions with a pK(a) in the range 3.0-3.8. Although the vesicular surface was determined to be highly negatively charged, treatment with neuraminidase had no effect on mobility and indicated that the relatively strong carboxyl groups of sialic acid do not contribute significantly to vesicular electrokinetic properties. Treatment of synaptic vesicles with trypsin or trypsinized concanavalin A resulted in increases in mobility, but treatment with ribonuclease, deoxyribonuclease, chrondroitinase ABC or hyaluronidase had no significant effect on mobility. Mn(2+) or Ca(2+) was more effective in decreasing vesicle mobility than was Mg(2+), Sr(2+) or Ba(2+). The electrokinetic properties of the synaptic vesicle surface are discussed and contrasted with the properties of the synaptosomal membrane.

Animals↗
PubMed1973

Molecules at the external nuclear surface. Sialic acid of nuclear membranes and electrophoretic mobility of isolated nuclei and nucleoli.

The molecules occurring as terminal residues on the external surfaces of nuclei prepared from rat liver by either sucrose-CaCl(2) or citric acid methods and nucleoli derived from the sucrose-CaCl(2) nuclei were studied chemically and electrokinetically. In 0.0145 M NaCl, 4.5% sorbitol, and 0.6 mM NaHCO(3) with pH 7.2 +/- 0.1 at 25 degrees C, the sucrose-CaCl(2) nuclei had an electrophoretic mobility of -1.92 microm/s/V/cm, the citric acid nuclei, -1.63 microm/s/V/cm, and the nucleoli, -2.53 microm/s/V/cm. The citric acid nuclei and the nucleoli contained no measurable sialic acid. The sucrose-CaCl(2) nuclei contained 0.7 nmol of sialic acid/mg nuclear protein; this was essentially located in the nuclear envelope. Treatment of these nuclei with 50 microg neuraminidase/mg protein resulted in release of 0.63 nmol of sialic acid/mg nuclear protein; treatment with 1 % trypsin caused release of 0.39 nmol of the sialic acid/mg nuclear protein. The pH-mobility curves for the particles indicated the sucrose-CaCl(2) nuclei surface had an acid-dissociable group of pK. approximately 2.7 while the pK for the nucleoli was considerably lower. Nucleoli treated with 50 microg neuraminidase/mg particle protein had a mobility of -2.53 microm/s/V/cm while sucrose-CaCl(2) nuclei similarly treated had a mobility of -1.41 microm/s/V/cm. Hyaluronidase at 50 microg/mg protein had no effect on nucleoli mobility but decreased the sucrose-CaCl(2) nuclei mobility to -1.79 microm/s/V/cm. Trypsin at 1 % elevated the electrophoretic mobility of the sucrose-CaCl(2) nuclei slightly but decreased the mobility of the nucleoli to -2.09 microm/s/V/cm. DNase at 50 microg/mg protein had no effect on the mobility of the isolated sucrose-CaCl(2) nuclei but decreased the electrophoretic mobility of the nucleoli to -1.21 microm/s/V/cm. RNase at 50 microg/mg protein also had no effect on the electrophoretic mobility of the sucrose-CaCl(2) nuclei but decreased the nucleoli mobility to -2.10 microm/s/V/cm. Concanavalin A at 50 microg/mg protein did not alter the nucleoli electrophoretic mobility but decreased the sucrose-CaCl(2) nuclei electrophoretic mobility to -1.64 microm/s/V/cm. The results are interpreted to mean that the sucrose-CaCl(2) nuclear external surface contains terminal sialic acid residues in trypsin-sensitive glycoproteins, contains small amounts of hyaluronic acid, is completely devoid of nucleic acids, and binds concanavalin A. The nucleolus surface is interpreted to contain a complex made up of protein, RNA, and primarily DNA, to be devoid of sialic acid and hyaluronic acid, and not to bind concanavalin A.

Animals↗