Activation of spinach pullulanase by reduction results in a decrease in the number of isomeric forms

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1548, Issue 2, 2001, Pages 175-186

  Schindler, Ilka ^a   Renz, Andreas ^b   Schmid, Franz X ^a   Beck, Erwin ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

^b BASF SE   (Germany)

Author keywords

Isomeric form; Limit dextrinase; Microheterogeneity; Pullulanase; Spinach

Indexed keywords

DISULFIDE; GLUTATHIONE; ISOENZYME; PEPTIDE; PULLULANASE; REDUCING AGENT; STARCH; THIOL GROUP; TRIS(2 CARBOXYETHYL)PHOSPHINE; TRYPSIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CHLOROPLAST; CHROMATOFOCUSING; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME INACTIVATION; ENZYME METABOLISM; ENZYME STRUCTURE; PEPTIDE SYNTHESIS; PLANT LEAF; PRIORITY JOURNAL; PROTEIN DEGRADATION; REDUCTION; SPINACH; STRUCTURE ACTIVITY RELATION;

CHLOROPLASTS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME ACTIVATION; GLUTATHIONE; GLYCOSIDE HYDROLASES; ISOENZYMES; MODELS, MOLECULAR; OXIDATION-REDUCTION; SPINACIA OLERACEA; TRYPSIN;

SPINACIA OLERACEA;

EID: 0035855205     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(01)00228-X     Document Type: Article

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