Enzymatic and immunological properties of alkaline phosphatase of bullfrog
β Scribed by Goseki, M. ;Oida, S. ;Sasaki, S.
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 476 KB
- Volume
- 254
- Category
- Article
- ISSN
- 0022-104X
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
Enzymatic and immunological properties of alkaline phosphatase (ALPase) in several tissues of bullfrog (Rana catesbiana) were investigated. Inhibition and thermal inactivation studies showed that bullfrog ALPases in kidney, liver, and intestine had similar enzymatic properties. In addition, mouse antiserum against bullfrog liver ALPase crossβreacted with kidney and intestine enzymes as well as with liver enzyme. These results suggest that a single phenotype of ALPase exists in all tissues of bullfrog in contrast to two or three isoenzymes in mammals.
π SIMILAR VOLUMES
Two clones of monoclonal antibodies against swine alkaline phosphatase (ALPase; orthophosphoric monoester phosphohydrolase, alkaline optimum, EC 3.1.3.1), which were useful in distinguishing human kidney and bone ALPases from liver ALPase, were successfully raised in mice. On the other hand, polyclo
Neutrophil alkaline phosphatase (NAP) was analysed in 25 pregnant women with trisomy 21 foetuses whose chromosomal aberration was recognized by cytogenetic study after amniocentesis. Enzyme investigation was performed at 20-22 weeks of gestation using cytochemical and biochemical techniques. Twenty-