A single domain of human prostatic acid phosphatase shows antibody-mediated restoration of catalytic activity

B. K. Choe, M. K. Dong, D. Walz, S. Gleason, N. R. Rose

Research output: Contribution to journalArticlepeer-review

Abstract

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 suggests that Sp3 is the enzymatically active domain of prostatic acid phosphatase.

Original languageEnglish (US)
Pages (from-to)6052-6055
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume79
Issue number19 I
DOIs
StatePublished - Dec 1 1982

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'A single domain of human prostatic acid phosphatase shows antibody-mediated restoration of catalytic activity'. Together they form a unique fingerprint.

Cite this