Equilibrium unfolding of dimeric human prostatic acid phosphatase involves an inactive monomeric intermediate

International Journal of Biological Macromolecules

Volumn 32, Issue 1-2, 2003, Pages 43-54

  Wójciak, Paulina ^a   Mazurkiewicz, Aleksandra ^a   Bakalova, Anastasia ^b   Kuciel, Radoslawa ^a  

^a JAGIELLONIAN UNIVERSITY MEDICAL COLLEGE   (Poland)

^b INSTITUTE OF MOLECULAR BIOLOGY   (Bulgaria)

Author keywords

Dimer; Folding intermediates; Prostatic acid phosphatase; Protein denaturation; Protein folding

Indexed keywords

2 (4' MALEIMIDOANILINO)NAPHTHALENE 6 SULFONATE; 8 ANILINO 1 NAPHTHALENESULFONIC ACID; ACID PHOSPHATASE PROSTATE ISOENZYME; DIMER; GUANIDINE; M PROTEIN; MONOMER; OLIGOMER; PHOSPHATASE; REAGENT; SULFONIC ACID DERIVATIVE; THIOL GROUP; TRYPTOPHAN; UNCLASSIFIED DRUG;

ANALYTICAL PARAMETERS; ARTICLE; BINDING AFFINITY; CATALYSIS; CHEMICAL REACTION; CHEMICAL STRUCTURE; CONCENTRATION (PARAMETERS); DIMERIZATION; DISSOCIATION; ENERGY; ENZYME ACTIVITY; ENZYME STABILITY; ENZYME SUBUNIT; FLUORESCENCE; GEL PERMEATION CHROMATOGRAPHY; HYDROPHOBICITY; MOLECULAR WEIGHT; PROTEIN CONFORMATION; PROTEIN FOLDING; SURFACE PROPERTY;

EID: 0344519692     PISSN: 01418130     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-8130(03)00024-2     Document Type: Article

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