Antigenic structure of adenylate kinase from porcine skeletal muscle. I. Three immunochemically active peptides obtained by cleavage with cyanogen bromide.

Abstract:

:Analysis of the quantitative precipitin reaction of adenylate kinase from porcine skeletal muscle with goat anti-adenylate kinase antiserum indicated that there are at least four antigenic determinants on the enzyme molecule. Porcine adenylate kinase was cleaved with cyanogen bromide, and four peptides were fractionated by ion-exchange chromatographies. Three fragments, CBb (2-56), CBfN (81-125), and CBfC (126-194), inhibited the quantitative precipitin reaction of intact adenylate kinase with goat antiserum. CBb, CBfN, and CBfC also inhibited the binding of 125I-labeled adenylate kinase to the specific antibody purified from goat antiserum. In both inhibition studies, the inhibitory activity of each fragment was extremely high, and reached 70% or more in the latter case. From these results and in view of the presence of the sequence -Glu-Glu-X-X'-Lys (or Arg)-Lys- in each immunochemically active fragment, we suggest that these fragments have similar antigenic determinants which are cross-reactive.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Sato N,Koyama Y,Shiokawa H

doi

10.1093/oxfordjournals.jbchem.a133867

subject

Has Abstract

pub_date

1982-05-01 00:00:00

pages

1749-57

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

91

pub_type

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