Prolyl 4-Hydroxylase from Human Placenta. Simultaneous Isolation of Immunoglobulin G which Binds to Ascaris Cuticle Collagen Academic Article uri icon

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 11,000-fold. An incidental 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. 1982, Gustav Fischer Verlag, Stuttgart/New York. All rights reserved.

published proceedings

  • Collagen and Related Research

author list (cited authors)

  • Guzman, N. A., Oronsky, A. L., Suarez, G., Meyerson, L. R., Cutroneo, K. R., Olsen, B. R., & Prockop, D. J.

citation count

  • 7

complete list of authors

  • Guzman, Norberto A||Oronsky, Arnold L||Suarez, Gerardo||Meyerson, Laurence R||Cutroneo, Kenneth R||Olsen, Bjørn R||Prockop, Darwin J

publication date

  • January 1982