Document Detail

Pig brain aldose reductase: purification, significance of the amino acid composition, substrate specificity and mechanism.
MedLine Citation:
PMID:  3121406     Owner:  NLM     Status:  MEDLINE    
1. Pig brain aldose reductase (ALR2, EC has been purified from fresh tissue with a approximately 60% improvement in specific activity over an acetone-powder preparation. 2. Dead-end inhibition and alternate substrate studies rule out an iso Theorell-Chance mechanism but are compatible with an ordered bi bi mechanism where NADPH and NADP+ function as the outside reactants in the direction of xylitol formation. 3. Subtle but significant differences are shown to exist in the distribution of apolar and mixed amino acid residues between aldose and aldehyde reductases when the mean fractional area loss [Rose et al., 1985] is used as the measure of compositional relatedness.
H Yoo; E T McGuinness
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The International journal of biochemistry     Volume:  19     ISSN:  0020-711X     ISO Abbreviation:  Int. J. Biochem.     Publication Date:  1987  
Date Detail:
Created Date:  1988-02-12     Completed Date:  1988-02-12     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0250365     Medline TA:  Int J Biochem     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  865-71     Citation Subset:  IM    
Department of Chemistry, Seton Hall University, South Orange, NJ 07079.
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MeSH Terms
Aldehyde Reductase / isolation & purification*,  metabolism
Amino Acids / analysis
Brain / enzymology*
Chromatography, Affinity
Chromatography, Ion Exchange
Substrate Specificity
Sugar Alcohol Dehydrogenases / isolation & purification*
Reg. No./Substance:
0/Amino Acids; EC 1.1.-/Sugar Alcohol Dehydrogenases; EC Reductase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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