Antibody restores catalytic activity of a small molecular weight fragment of human prostatic acid phosphatase

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

Research output: Contribution to journalArticle

Abstract

Human prostatic acid phosphatase was dissociated into subunits and the subunits further cleaved by cyanogen bromide. The subunits and cyanogen bromide-derived peptides were catalytlcally inactive. In the presence of specific antibodies directed against human prostatic acid phosphatase, both the subunit polypeptides and one of the cyanogen bromide-derived peptides (C5) regained catalytic activity.

Original languageEnglish (US)
Pages (from-to)451-454
Number of pages4
JournalMolecular Immunology
Volume18
Issue number5
DOIs
StatePublished - 1981
Externally publishedYes

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Catalytic Antibodies
Cyanogen Bromide
Molecular Weight
Peptides
Antibodies
prostatic acid phosphatase

ASJC Scopus subject areas

  • Molecular Biology
  • Immunology

Cite this

Antibody restores catalytic activity of a small molecular weight fragment of human prostatic acid phosphatase. / Choe, B. K.; Dong, M.; Walz, D.; Rose, N. R.

In: Molecular Immunology, Vol. 18, No. 5, 1981, p. 451-454.

Research output: Contribution to journalArticle

Choe, B. K. ; Dong, M. ; Walz, D. ; Rose, N. R. / Antibody restores catalytic activity of a small molecular weight fragment of human prostatic acid phosphatase. In: Molecular Immunology. 1981 ; Vol. 18, No. 5. pp. 451-454.
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