Open AccessA single domain of human prostatic acid phosphatase shows antibody-mediated restoration of catalytic activity.
Author(s) -
B. K. Choe,
MengJie Dong,
Daniel A. Walz,
S L Gleason,
Noel R. Rose
Publication year - 1982
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.79.19.6052
Subject(s) - acid phosphatase , prostatic acid phosphatase , chemistry , phosphatase , biochemistry , proteolysis , enzyme , antibody , tartrate , antigen , protease , microbiology and biotechnology , biology , immunology
By limited proteolysis with mouse submaxillaris protease, human prostatic acid phosphatase (EC 3.1.3.2) was cleaved into three fragments, Sp1, Sp2, and Sp3, which individually had no enzymatic activity. One of the fragments, Sp3, regained enzymatic activity after interaction with rabbit antibody to prostatic acid phosphatase. The Sp3 fragment was purified and characterized as to its molecular weight, amino acid composition, and carbohydrate content. The Sp3 fragment behaved like the parent molecule in L(+)-tartrate affinity and in trapping of a phosphoryl intermediate. The same Sp3 fragment also bears the most prominent antigenic determinants. This evidence suggest that Sp3 is the enzymatically active domain of prostatic acid phosphatase.