Heterogeneity of liver acid phosphatases in developing chick embryo

Wang, K.-M.

doi:10.1042/bj1150191

Cited by 18 publications

(2 citation statements)

References 16 publications

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“…The enzymic activities of both parasites were moderately inhibited by 10~2 M cysteine, indicating that both the phosphatases are independent of reduced thiol groups. The inhibition of acid phosphatase by cysteine has also been reported by Wang (1969) in the liver of developing chick embryo.…”

Section: Discussionmentioning

confidence: 77%

Phosphatase systems in Fasciolopsis buski Lankester, 1857 and Gastrodiscus aegyptiacus Cobbold, 1876

Goil

1973

Parasitology

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Biochemical studies on the non-specific phosphomonoesterases have demonstrated the presence of acid phosphomonoesterase with maximum activity at pH 4·0 in Gastrodiscus aegyptiacus (enzyme I) and at pH 4·5 in the case of Fasdolopsis buski (enzyme II). The Km for ρ-nitrophenyl phosphate hydrolysis was 0·66 mM for enzyme I and 1·1 mM for enzyme II. Different concentrations of fluoride, arsenate, tartrate, tartaric acid, cysteine and copper brought about inhibition of both enzymes and magnesium, iodoaeetate, iodoacetamide and EDTA had no influence on either enzyme activity. Cobalt activated both enzymes while zinc inhibited enzyme I and strongly stimulated enzyme II.

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Section: Discussionmentioning

confidence: 77%

Phosphatase systems in Fasciolopsis buski Lankester, 1857 and Gastrodiscus aegyptiacus Cobbold, 1876

Goil

1973

Parasitology

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“…The developing mouse duodenum has been extensively used for studies on both normal changes and substrate-or hormoneinduced increases of alkaline phosphatase levels (10,26,27). Developmental changes in other intestinal phosphatase activities have been examined in the chicken (37,38), and studies have been made of developmental changes in levels of glucose-6-phosphatase (EC 3.1.3.9) in rat liver (12,40) and chick liver (17,34,37), of acid phosphatase (EC 3.1.3.2) and inorganic pyrophosphatase (EC 3.6.1.1) in rat liver (35) and chick liver (37), and of various p-nitrophenyl phosphatase activities in chick liver (37,41).…”

mentioning

confidence: 99%

Development of Disaccharidase and Phosphatase Activities in the Intestine and Liver

Cf¹

1973

Enzyme Protein

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Changes in specific activity levels of disaccharidases in the intestine and of phosphatases in liver and intestine were studied during development of the chick embryo and chick. A diversity of developmental patterns were observed among the various enzymes. However, many of the intestinal enzyme activities showed marked increases about the time of hatching, and some declined rapidly from transient peaks shortly after hatching. Most of the hepatic enzyme activities were present at relatively high levels in the embryo and showed modest changes from these levels about the time of hatching. Hydrocortisone administration to embryos evoked premature increases of a number of intestinal enzymes, but resulted in substantial reduction of several hepatic enzyme activities. The different patterns of enzymic differentiation in the two tissues are discussed.

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Purification and subcellular localization of Zn‐dependent acid p‐nitrophenylphosphatase in frog liver and comparison with other vertebrates

et al. 1990

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Zn2(+)-dependent acid p-nitrophenylphosphatase (Zn-AcPase) from liver of Rana esculenta was purified to homogeneity. The purified enzyme moves as a single electrophoretic band at pH 8.3 in 7.5% acrylamide and was coincident with the enzyme activity. The enzyme has a molecular weight of 102,000 +/- 5,000D and is a dimer with two apparently similar polypeptide chains of 48,000 +/- 3,000D as determined by sodium dodecylsulfate gel electrophoresis. Zn-AcPase from frog liver requires Zn2+ ions for catalytic activity; other bivalent cations have little or no effect. The enzyme with a pI of 7.07 does not appear to be a glycoprotein and was associated with the soluble fraction after liver cell fractionation. The biochemical and molecular properties of frog liver Zn-AcPase were compared with that of the enzyme partially purified from carp (Cyprinus carpio), pike (Esox lucius), and rat (Rattus norvegicus).

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Heterogeneity of liver acid phosphatases in developing chick embryo

Cited by 18 publications

References 16 publications

Phosphatase systems in Fasciolopsis buski Lankester, 1857 and Gastrodiscus aegyptiacus Cobbold, 1876

Phosphatase systems in Fasciolopsis buski Lankester, 1857 and Gastrodiscus aegyptiacus Cobbold, 1876

Development of Disaccharidase and Phosphatase Activities in the Intestine and Liver

Purification and subcellular localization of Zn‐dependent acid p‐nitrophenylphosphatase in frog liver and comparison with other vertebrates

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