Literature DB >> 4028682

Erythrocyte acid phosphatase: species specificity in activity modulation by purine analogs.

J M Naidu, H W Mohrenweiser.   

Abstract

The previous studies of the interaction of purine analogs and human erythrocyte acid phosphatase isozymes were extended to include erythrocyte acid phosphatase from seven other species. Consistent responses, similar to the observations with the several genotypically different human isozymes, were observed. The isozyme from chimpanzee erythrocytes was similar to the human B-type isozyme while the baboon and cow isozymes were at the other extreme in responsiveness and were more divergent from the B-isozyme than was the human A-type isozyme. The ACP from rabbit, dog, sheep and rhesus erythrocytes exhibited intermediate levels of responsiveness but did differ from the human A-type isozyme. Additional studies indicated some differences between the responsiveness of the partially purified erythrocyte enzyme and the low molecular weight ACP from liver.

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Year:  1985        PMID: 4028682     DOI: 10.1016/0305-0491(85)90375-x

Source DB:  PubMed          Journal:  Comp Biochem Physiol B        ISSN: 0305-0491


  1 in total

1.  Studies of the purine analog associated modulation of human erythrocyte acid phosphatase activity.

Authors:  K H Wurzinger; J E Novotny; H W Mohrenweiser
Journal:  Mol Cell Biochem       Date:  1985-03       Impact factor: 3.396

  1 in total

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