Two antigenic sites of tissue transglutaminase

L. Fésüs, K. Laki

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

The immunization of rabbits with purified guinea pig liver transglutaminase resulted in the appearance of two antibody populations against the enzyme: one which reacted only with the Ca2+-enzyme complex and another which reacted with the intact as well as the Ca2+-enzyme. The Ca2+-induced conformational change of the enzyme molecule exposes a new antigenic determinant which initiates the production of a specific antibody population. When the glutamine substrate of the enzyme was a dipeptide, the result of the interaction of the Ca2+-enzyme and its isolated specific antibody was an apparent activation of the catalytic activity. However, when protein substrates were used, an inhibition was observed. The characterization of the mechanism of the activation and the inhibition has led to the conclusion that the consequence of the interaction of the Ca2+-enzyme and its specific antibody is not only a limited steric hindrance of the active center but, besides that, a stabilization of the otherwise labile Ca2+-enzyme. The other antibody population reacts with both forms of the enzyme and its inhibitory effect, which has been observed in each assay, could be due to a prevention of the Ca2+-induced formation of the active enzyme.

Original languageEnglish
Pages (from-to)4061-4066
Number of pages6
JournalBiochemistry
Volume16
Issue number18
Publication statusPublished - 1977

Fingerprint

Enzymes
Antibodies
Chemical activation
transglutaminase 2
Population
Immunization
Transglutaminases
Dipeptides
Substrates
Glutamine
Liver
Epitopes
Assays
Catalyst activity
Guinea Pigs
Stabilization
Rabbits
Molecules
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Two antigenic sites of tissue transglutaminase. / Fésüs, L.; Laki, K.

In: Biochemistry, Vol. 16, No. 18, 1977, p. 4061-4066.

Research output: Contribution to journalArticle

Fésüs, L & Laki, K 1977, 'Two antigenic sites of tissue transglutaminase', Biochemistry, vol. 16, no. 18, pp. 4061-4066.
Fésüs, L. ; Laki, K. / Two antigenic sites of tissue transglutaminase. In: Biochemistry. 1977 ; Vol. 16, No. 18. pp. 4061-4066.
@article{546ee7c0d8c9485a95b80b610d1f267f,
title = "Two antigenic sites of tissue transglutaminase",
abstract = "The immunization of rabbits with purified guinea pig liver transglutaminase resulted in the appearance of two antibody populations against the enzyme: one which reacted only with the Ca2+-enzyme complex and another which reacted with the intact as well as the Ca2+-enzyme. The Ca2+-induced conformational change of the enzyme molecule exposes a new antigenic determinant which initiates the production of a specific antibody population. When the glutamine substrate of the enzyme was a dipeptide, the result of the interaction of the Ca2+-enzyme and its isolated specific antibody was an apparent activation of the catalytic activity. However, when protein substrates were used, an inhibition was observed. The characterization of the mechanism of the activation and the inhibition has led to the conclusion that the consequence of the interaction of the Ca2+-enzyme and its specific antibody is not only a limited steric hindrance of the active center but, besides that, a stabilization of the otherwise labile Ca2+-enzyme. The other antibody population reacts with both forms of the enzyme and its inhibitory effect, which has been observed in each assay, could be due to a prevention of the Ca2+-induced formation of the active enzyme.",
author = "L. F{\'e}s{\"u}s and K. Laki",
year = "1977",
language = "English",
volume = "16",
pages = "4061--4066",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "18",

}

TY - JOUR

T1 - Two antigenic sites of tissue transglutaminase

AU - Fésüs, L.

AU - Laki, K.

PY - 1977

Y1 - 1977

N2 - The immunization of rabbits with purified guinea pig liver transglutaminase resulted in the appearance of two antibody populations against the enzyme: one which reacted only with the Ca2+-enzyme complex and another which reacted with the intact as well as the Ca2+-enzyme. The Ca2+-induced conformational change of the enzyme molecule exposes a new antigenic determinant which initiates the production of a specific antibody population. When the glutamine substrate of the enzyme was a dipeptide, the result of the interaction of the Ca2+-enzyme and its isolated specific antibody was an apparent activation of the catalytic activity. However, when protein substrates were used, an inhibition was observed. The characterization of the mechanism of the activation and the inhibition has led to the conclusion that the consequence of the interaction of the Ca2+-enzyme and its specific antibody is not only a limited steric hindrance of the active center but, besides that, a stabilization of the otherwise labile Ca2+-enzyme. The other antibody population reacts with both forms of the enzyme and its inhibitory effect, which has been observed in each assay, could be due to a prevention of the Ca2+-induced formation of the active enzyme.

AB - The immunization of rabbits with purified guinea pig liver transglutaminase resulted in the appearance of two antibody populations against the enzyme: one which reacted only with the Ca2+-enzyme complex and another which reacted with the intact as well as the Ca2+-enzyme. The Ca2+-induced conformational change of the enzyme molecule exposes a new antigenic determinant which initiates the production of a specific antibody population. When the glutamine substrate of the enzyme was a dipeptide, the result of the interaction of the Ca2+-enzyme and its isolated specific antibody was an apparent activation of the catalytic activity. However, when protein substrates were used, an inhibition was observed. The characterization of the mechanism of the activation and the inhibition has led to the conclusion that the consequence of the interaction of the Ca2+-enzyme and its specific antibody is not only a limited steric hindrance of the active center but, besides that, a stabilization of the otherwise labile Ca2+-enzyme. The other antibody population reacts with both forms of the enzyme and its inhibitory effect, which has been observed in each assay, could be due to a prevention of the Ca2+-induced formation of the active enzyme.

UR - http://www.scopus.com/inward/record.url?scp=0017400946&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017400946&partnerID=8YFLogxK

M3 - Article

C2 - 71918

AN - SCOPUS:0017400946

VL - 16

SP - 4061

EP - 4066

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 18

ER -