Literature DB >> 1464109

Three types of membranous ATPase on rat liver lysosomes.

H Hayashi1, K Arai, O Sato, A Shimaya, Y Sai, S Ohkuma.   

Abstract

At least three types of vanadate-insensitive membranous ATPase were identified on rat liver lysosomes: bafilomycin A1-sensitive Mg(2+)-ATPase (H(+)-ATPase), N-ethylmaleimide (NEM)-sensitive but bafilomycin A1-insensitive Mg(2+)-ATPase (ATPase I), and NEM-insensitive Ca2+/Mg(2+)-ATPase (ATPase II). They showed different sensitivity to chemicals and ions with apparent molecular masses of 700-800, 500-650, and 360 kDa, respectively. Of these membranous ATPases, H(+)-ATPase seemed to constitute only one tenth of the ATPase activity on rat liver lysosomes and to be the only ATPase that exposed its active site to the cytoplasmic side of the lysosomal membranes.

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Year:  1992        PMID: 1464109     DOI: 10.1248/cpb.40.2783

Source DB:  PubMed          Journal:  Chem Pharm Bull (Tokyo)        ISSN: 0009-2363            Impact factor:   1.645


  2 in total

1.  Preconditioning rabbit cardiomyocytes: role of pH, vacuolar proton ATPase, and apoptosis.

Authors:  R A Gottlieb; D L Gruol; J Y Zhu; R L Engler
Journal:  J Clin Invest       Date:  1996-05-15       Impact factor: 14.808

2.  ATP stimulates lysosomal sulphate transport at neutral pH: evidence for phosphorylation of the lysosomal sulphate carrier.

Authors:  H F Chou; M Passage; A J Jonas
Journal:  Biochem J       Date:  1997-11-01       Impact factor: 3.857

  2 in total

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