Immuno-affinity purification of specific antibodies against human gastrin releasing peptide (h-GRP) by the h-GRP(1-8)-linked polydimethylacrylamide resin

Int J Pept Protein Res. 1989 Jun;33(6):457-62. doi: 10.1111/j.1399-3011.1989.tb00223.x.

Abstract

A new method for immuno-affinity purification of specific antibodies against human gastrin releasing peptide(h-GRP) was developed. The antiserum GP(No. 6201) elicited by h-GRP-BSA conjugate was heterogeneous and reacted not only with h-GRP and its fragments but also partially with other structurally related peptides, such as other GRPs (porcine, canine, and chicken), bombesin, and neuromedin-C. To obtain specific antibodies against human GRP, antiserum GP was purified by column chromatography on the amino-terminal octapeptide h-GRP(1-8)-linked polydimethylacrylamide resin. The antibody thus obtained was highly specific to amino-terminal sequence of h-GRP and hardly reacted with other GRPs (porcine, canine and chicken), bombesin, and even carboxy-terminal h-GRP fragments in ELISA.

MeSH terms

  • Acrylamides
  • Amino Acid Sequence
  • Animals
  • Antibodies / isolation & purification*
  • Antibody Specificity
  • Chromatography, Affinity
  • Enzyme-Linked Immunosorbent Assay
  • Gastrin-Releasing Peptide
  • Gastrins / immunology*
  • Humans
  • Molecular Sequence Data
  • Peptides / immunology*
  • Resins, Plant
  • Species Specificity

Substances

  • Acrylamides
  • Antibodies
  • Gastrins
  • Peptides
  • Resins, Plant
  • Gastrin-Releasing Peptide