Literature DB >> 1003114

Separation of arginase isoenzymes from human tissues by agar gel electrophoresis.

O Borcić, B Straus.   

Abstract

Arginase (EC 3.5.3.1) from human liver. kidney, mammary gland, and erythrocytes, was separated by agar-gel electrophoresis using barbital buffer pH 8.6. Three isoenzymes were separated. Two of these, A2 and A3, occur in liver and erythrocytes. The same two isoenzymes were found in the kidney, but in reversed proportions. In addition to the A3 isoenzyme, the mammary gland contains a fast anodically moving A1 isoenzyme. The three isoenzymes differ in their degree of sensitivity to ornithine.

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Year:  1976        PMID: 1003114

Source DB:  PubMed          Journal:  J Clin Chem Clin Biochem        ISSN: 0340-076X


  3 in total

1.  Binding of α,α-disubstituted amino acids to arginase suggests new avenues for inhibitor design.

Authors:  Monica Ilies; Luigi Di Costanzo; Daniel P Dowling; Katherine J Thorn; David W Christianson
Journal:  J Med Chem       Date:  2011-07-18       Impact factor: 7.446

2.  2-aminoimidazole amino acids as inhibitors of the binuclear manganese metalloenzyme human arginase I.

Authors:  Monica Ilies; Luigi Di Costanzo; Michelle L North; Jeremy A Scott; David W Christianson
Journal:  J Med Chem       Date:  2010-05-27       Impact factor: 7.446

3.  Immunohistochemical localisation of arginase in human liver using monoclonal antibodies against human liver arginase.

Authors:  H Multhaupt; P Fritz; K Schumacher
Journal:  Histochemistry       Date:  1987
  3 in total

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