Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Evaluation of serum γ-glutamyltransferase by electrofocusing, and variations in isoform patterns

Lilja, H. LU orcid ; Jeppsson, J. O. LU and Kristensson, H. (1983) In Clinical Chemistry 29(6). p.1034-1037
Abstract

Serum γ-glutamyltransferase (EC 2.3.2.2) showed microheterogeneity on electrofocusing, owing to variations in sialic acid content. We investigated the isoform patterns of papain-treated serum samples on agarose gels containing nonionic detergent and ampholytes in the low pH range. Serum from cases of cholestasis show seven bands with γ-glutamyltransferase activity. These same bands were also found in liver tissue similarly treated, and they had pl values ranging from 3.8 to 4.2. Papain-treated sera that also had been neuraminidase digested showed only a single band, still enzymatically active and with a pI of 5.9. Increased γ-glutamyltransferase in serum as a result of alcoholic abuse was combined with a abnormally high degree of... (More)

Serum γ-glutamyltransferase (EC 2.3.2.2) showed microheterogeneity on electrofocusing, owing to variations in sialic acid content. We investigated the isoform patterns of papain-treated serum samples on agarose gels containing nonionic detergent and ampholytes in the low pH range. Serum from cases of cholestasis show seven bands with γ-glutamyltransferase activity. These same bands were also found in liver tissue similarly treated, and they had pl values ranging from 3.8 to 4.2. Papain-treated sera that also had been neuraminidase digested showed only a single band, still enzymatically active and with a pI of 5.9. Increased γ-glutamyltransferase in serum as a result of alcoholic abuse was combined with a abnormally high degree of sialylation of the enzyme, giving more anodal isoforms. The decline in the concentration of this enzyme during several weeks of abstinence was accompanied by a gradual decrease in γ-glutamyltransferase sialylation and the appearance of more cathodal fractions.

(Less)
Please use this url to cite or link to this publication:
author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Clinical Chemistry
volume
29
issue
6
pages
1034 - 1037
publisher
American Association for Clinical Chemistry
external identifiers
  • pmid:6133655
  • scopus:0020630845
ISSN
0009-9147
DOI
10.1093/clinchem/29.6.1034
language
English
LU publication?
yes
id
fe598bdf-6655-49f1-b726-0adcbcc5d253
date added to LUP
2022-12-06 16:55:47
date last changed
2024-01-03 19:31:05
@article{fe598bdf-6655-49f1-b726-0adcbcc5d253,
  abstract     = {{<p>Serum γ-glutamyltransferase (EC 2.3.2.2) showed microheterogeneity on electrofocusing, owing to variations in sialic acid content. We investigated the isoform patterns of papain-treated serum samples on agarose gels containing nonionic detergent and ampholytes in the low pH range. Serum from cases of cholestasis show seven bands with γ-glutamyltransferase activity. These same bands were also found in liver tissue similarly treated, and they had pl values ranging from 3.8 to 4.2. Papain-treated sera that also had been neuraminidase digested showed only a single band, still enzymatically active and with a pI of 5.9. Increased γ-glutamyltransferase in serum as a result of alcoholic abuse was combined with a abnormally high degree of sialylation of the enzyme, giving more anodal isoforms. The decline in the concentration of this enzyme during several weeks of abstinence was accompanied by a gradual decrease in γ-glutamyltransferase sialylation and the appearance of more cathodal fractions.</p>}},
  author       = {{Lilja, H. and Jeppsson, J. O. and Kristensson, H.}},
  issn         = {{0009-9147}},
  language     = {{eng}},
  number       = {{6}},
  pages        = {{1034--1037}},
  publisher    = {{American Association for Clinical Chemistry}},
  series       = {{Clinical Chemistry}},
  title        = {{Evaluation of serum γ-glutamyltransferase by electrofocusing, and variations in isoform patterns}},
  url          = {{http://dx.doi.org/10.1093/clinchem/29.6.1034}},
  doi          = {{10.1093/clinchem/29.6.1034}},
  volume       = {{29}},
  year         = {{1983}},
}