Enzyme.
Discontinued
Publisher:
Karger.. Basel : Karger
Frequency: Six no. a year
Country: Switzerland
Language: English
Author(s):
International Society for Clinical Enzymology.
Start Year:1971 - 1992
Identifiers
| ISSN: | 0013-9432 (Print) 0013-9432 (Linking) |
| NLM ID: | 1262265 |
| (DNLM): | E10780000(s) |
| (OCoLC): | 01568103 |
| Coden: | ENZYBT |
| Classification: | W1 EN986N |
Structural aspects of the plasminogen of various species. The N-terminal amino acid sequence of equine, ovine, canine, goat and rabbit plasminogen were determined and compared with those already known of the human, bovine, porcine and feline molecule. Furthermore, the kringle 4 domains of equine, ovine, canine and goat plasminogen, prepared by limited cleavage with elastase, were sequenced and compared with the known species of human, bovine, porcine and chicken plasminogen. Homology with the human kringle 4 ranges between 73% (chicken) and 90% (bovine). Comparison of sequences, fragmentation patterns with elastase and adsorption on lysine-Bio-Gel su...
Transfer of gamma-glutamyltransferase from mother colostrum to newborn goat and foal. In goat and mare colostrum, gamma-glutamyltransferase (GGT) activity is relatively low (mean values are, respectively, 900 and 350 U/l). In the serum of newborns before suckling, GGT is also low (less than or equal to 28 U/l in goats and less than or equal to U/l in foals); then in goats GGT is much increased on the 1st day (mean = 127 U/l), and it decreases during the following days. In foals, serum GGT slowly but regularly increases for the first 5 days, then decreases. Such differences can be attributed to intestinal protein absorption capabilities which are selective in newborn foals and u...
Intestinal alkaline phosphatase-like properties of horse kidney alkaline phosphatase. Two isoenzymes of alkaline phosphatase from horse kidney were identified by cellulose acetate electrophoresis. Horse kidney alkaline phosphatase was similar to horse intestinal alkaline phosphatase, in regard to both antigenicity and response to levamisole inhibition, but different from horse liver alkaline phosphatase. This study suggests that horse kidney alkaline phosphatase is an expression of the intestinal gene locus and not the hepatic gene locus.
Subcellular localization and properties of the NAD(P)H oxidase from equine polymorphonuclear leukocytes. The subcellular distribution of the superoxide-forming enzyme in horse polymorphonuclear leukocytes was investigated. After activation of the cells with sodium oleate, a relatively stable and NAD(P)H-dependent oxygen consumption and superoxide production was found in association with the plasma membranes. The pH dependence displayed an optimum near neutrality. The apparent Km values were 38 x 10(-6) mol/l for NADPH and 1,560 x 10(-6) mol/l for NADH, suggesting that NADPH is the physiological donor. The rates of oxygen uptake, O2- production, and NADP consumption were consistent with the stoich...
Subcellular distribution of particle-associated enzymes in horse neutrophil leukocytes. The subcellular components of purified neutrophil leukocytes from horse blood were fractionated by isopyknic equilibration in sucrose and metrizamide gradients. Five classes of particles have been identified: dense azurophil granules containing the bulk of the lysosomal acid hydrolase and peroxidase activity (A); less dense particles, containing all the lysozyme activity, but not resolved from a second population of azurophils B, and particles of low density, biochemically characterized as a plasma membrane fraction (C). Isopyknic equilibration in sucrose disclosed a minor membrane fraction (D...
The optimum pH of renal adenosine triphosphatase in rats: influence of vanadate, noradrenaline and potassium. In the presence of vanadate, the optimum pH of renal (Na+, K+)-ATPase in rats is reduced and lies in the range of intracellular pH. This explains the difference in optimum pH observed with ATP extracted from equine muscle. Removal of vanadate from such ATP (with noradrenaline) raises the optimum to the accepted range obtained with synthetic ATP. Changes in the sensitivity of the enzyme to potassium concentration contribute to the alterations in optimum pH. The optimum pH of Mg-ATPase is unaffected by vanadate. Since vanadate may be an intracellular regulator of (Na+, K+)-ATPase changes of opti...
Rapid heterolysis of indophenyl acetate by a constituent of a preparation of horse serum cholinesterase. A transient phase for the hydrolysis of indophenyl acetate by the commercial preparation of horse serum cholinesterase was observed on a stopped-flow spectrophotometer. It was found that the transient process is a reaction of the ester with a major component of the preparation and is not caused by the serum cholinesterase enzyme. This noncholinesterase component was isolated and the dependence of its concentration and that of the ester upon the transient liberation of the indophenolate ion were determined. Studies with the isolated component and subsequent analyses have led to the tentative id...
Acid phosphatase heterogeneity in horse neutrophil and eosinophil leukocytes. Two distinct groups of acid phosphatase containing granules were characterized in neutrophils, each group displaying different multiple forms of the enzyme. The heavy granule acid phosphatase showed a lysosomal location. A second lighter group of particles contained a thermolabile, thiol-dependent acid p-nitrophenyl and alpha-naphtylphosphatase, an enzyme clearly different from lysosomal acid phosphatase. Acid phosphatase activity from eosinophil leukocytes appeared to be totally associated with the typical eosinophil granules. On mechanical disruption of these particles, an acid phosphatase w...