Document Detail

Unique structural features of red kidney bean purple acid phosphatase.
MedLine Citation:
PMID:  7590853     Owner:  NLM     Status:  MEDLINE    
Purple acid phosphatase from red kidney beans (Phaseolus vulgaris) has been purified to homogeneity and characterized. The enzyme is a homodimer of 60 kDa subunits each containing one atom of zinc and iron in the active site. Circular dichroism spectral studies on the purified enzyme reveals that a large portion of the peptide backbone is in the unordered and beta-turn conformation. A unique feature of the red kidney bean acid phosphatase, which we have found, is that one of the two cysteines of each subunit is involved in the formation of an inter-subunit disulphide. The thiol group of the other cysteine is not necessary for the activity of the enzyme. Western blot analysis with antibodies raised against kidney bean acid phosphatase could not recognize acid phosphatases from other sources except from potato. This paper emphasizes the fact that acid phosphatases are functionally, but not structurally, conserved enzymes.
A G Cashikar; M N Rao
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Indian journal of biochemistry & biophysics     Volume:  32     ISSN:  0301-1208     ISO Abbreviation:  Indian J. Biochem. Biophys.     Publication Date:  1995 Jun 
Date Detail:
Created Date:  1995-11-28     Completed Date:  1995-11-28     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0310774     Medline TA:  Indian J Biochem Biophys     Country:  INDIA    
Other Details:
Languages:  eng     Pagination:  130-6     Citation Subset:  IM    
Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad, India.
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MeSH Terms
Acid Phosphatase / chemistry*,  isolation & purification
Fabaceae / enzymology*
Glycoproteins / chemistry*,  isolation & purification
Molecular Structure
Plant Proteins / chemistry*
Plants, Medicinal*
Reg. No./Substance:
0/Glycoproteins; 0/Plant Proteins; EC 3.1.3.-/purple acid phosphatase; EC Phosphatase

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