Prolyl 4-hydroxylase from human placenta. Simultaneous isolation of immunoglobulin G which binds to Ascaris cuticle collagen

N. A. Guzman, A. L. Oronsky, G. Suarez

Research output: Contribution to journalArticle

Abstract

Prolyl-4-hydroxylase, the enzyme which synthesizes the 4-hydroxyproline found in collagens, was purified from human placenta. For this purpose, a new purification procedure was developed. The procedure involves chromatography on two DEAE-cellulose columns in addition to the previously developed affinity column. The new procedure makes it possible to obtain homogenous enzyme from tissues which contain low concentrations of prolyl 4-hydroxylase. When applied to human placenta, the purification was about 1,000-fold. An 11,000-fold observation was that when the original affinity column procedure was applied to placenta, the eluted enzyme peak contained large amounts of immunoglobulin, probably immunoglobulin G. On the basis of this observation, a simple procedure was developed for purifying immunoglobulin from human placenta or plasma.

Original languageEnglish (US)
Pages (from-to)365-380
Number of pages16
JournalCollagen and Related Research
Volume2
Issue number5
StatePublished - 1982
Externally publishedYes

Fingerprint

Prolyl Hydroxylases
Ascaris
Placenta
Collagen
Immunoglobulin G
Immunoglobulins
Enzymes
DEAE-Cellulose
Hydroxyproline
Chromatography
Observation

ASJC Scopus subject areas

  • Rheumatology

Cite this

Prolyl 4-hydroxylase from human placenta. Simultaneous isolation of immunoglobulin G which binds to Ascaris cuticle collagen. / Guzman, N. A.; Oronsky, A. L.; Suarez, G.

In: Collagen and Related Research, Vol. 2, No. 5, 1982, p. 365-380.

Research output: Contribution to journalArticle

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