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The microheterogeneity of desialylated α1-antichymotrypsin : the occurrence of two amino-terminal isoforms, one lacking a His-Pro dipeptide

Lindmark, Bertil ; Lilja, Hans LU orcid ; Alm, Ragnar LU and Eriksson, Sten (1989) In Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 997(1-2). p.90-95
Abstract

ACT (α1-antichymotrypsin), a serine antiproteinase with specificity against neutrophil cathepsin G, is homologous with α1-antitrypsin, plasminogen activator inhibitor and angiotensinogen, all with known amino-terminal microheterogeneity. Here we report that the two predominant isoforms of desialylated ACT obtained on isoelectric focusing correspond to a microheterogeneity at the amino terminus of ACT: one isoform (His-Pro-Asn-Ser-Pro-) and a two residues shorter isoform (Asn-Ser-Pro-). The relative occurrence of the two isoforms was comparable both in normal plasma, acute-phase plasma and plasma from subjects with heterozygous familial ACT deficiency. When desialyllated ACT, isolated by affinity chromatography from... (More)

ACT (α1-antichymotrypsin), a serine antiproteinase with specificity against neutrophil cathepsin G, is homologous with α1-antitrypsin, plasminogen activator inhibitor and angiotensinogen, all with known amino-terminal microheterogeneity. Here we report that the two predominant isoforms of desialylated ACT obtained on isoelectric focusing correspond to a microheterogeneity at the amino terminus of ACT: one isoform (His-Pro-Asn-Ser-Pro-) and a two residues shorter isoform (Asn-Ser-Pro-). The relative occurrence of the two isoforms was comparable both in normal plasma, acute-phase plasma and plasma from subjects with heterozygous familial ACT deficiency. When desialyllated ACT, isolated by affinity chromatography from ACT-deficient, normal or acute-phase plasma, was compared with regard to mass and charge microheterogeneity, we found no significant differences in either respect. Nor was the isoform pattern of desialylated plasma from patients with rheumatoid arthritis different. Although the occurrence of heterozygous familial ACT deficiency implies genotypic variation, isolated ACT from patients with the trait was not found to exhibit any phenotypic variation detectable by standard electrophoretic methods.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Amino terminal amino acid sequence, Isoelectric focusing, Microheterogeneity, Serpin, α-Antichymotrypsin
in
Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
volume
997
issue
1-2
pages
90 - 95
publisher
Elsevier
external identifiers
  • pmid:2787670
  • scopus:0024382386
ISSN
0167-4838
DOI
10.1016/0167-4838(89)90139-8
language
English
LU publication?
yes
id
d07be5c9-8c26-4d8f-a94c-bf8ff3b1e220
date added to LUP
2022-12-06 17:04:43
date last changed
2024-01-03 19:32:27
@article{d07be5c9-8c26-4d8f-a94c-bf8ff3b1e220,
  abstract     = {{<p>ACT (α<sub>1</sub>-antichymotrypsin), a serine antiproteinase with specificity against neutrophil cathepsin G, is homologous with α<sub>1</sub>-antitrypsin, plasminogen activator inhibitor and angiotensinogen, all with known amino-terminal microheterogeneity. Here we report that the two predominant isoforms of desialylated ACT obtained on isoelectric focusing correspond to a microheterogeneity at the amino terminus of ACT: one isoform (His-Pro-Asn-Ser-Pro-) and a two residues shorter isoform (Asn-Ser-Pro-). The relative occurrence of the two isoforms was comparable both in normal plasma, acute-phase plasma and plasma from subjects with heterozygous familial ACT deficiency. When desialyllated ACT, isolated by affinity chromatography from ACT-deficient, normal or acute-phase plasma, was compared with regard to mass and charge microheterogeneity, we found no significant differences in either respect. Nor was the isoform pattern of desialylated plasma from patients with rheumatoid arthritis different. Although the occurrence of heterozygous familial ACT deficiency implies genotypic variation, isolated ACT from patients with the trait was not found to exhibit any phenotypic variation detectable by standard electrophoretic methods.</p>}},
  author       = {{Lindmark, Bertil and Lilja, Hans and Alm, Ragnar and Eriksson, Sten}},
  issn         = {{0167-4838}},
  keywords     = {{Amino terminal amino acid sequence; Isoelectric focusing; Microheterogeneity; Serpin; α-Antichymotrypsin}},
  language     = {{eng}},
  month        = {{07}},
  number       = {{1-2}},
  pages        = {{90--95}},
  publisher    = {{Elsevier}},
  series       = {{Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular}},
  title        = {{The microheterogeneity of desialylated α<sub>1</sub>-antichymotrypsin : the occurrence of two amino-terminal isoforms, one lacking a His-Pro dipeptide}},
  url          = {{http://dx.doi.org/10.1016/0167-4838(89)90139-8}},
  doi          = {{10.1016/0167-4838(89)90139-8}},
  volume       = {{997}},
  year         = {{1989}},
}