Publication Date:
1978-09-29
Description:
The Z variant of alpha1-antitrypsin was isolated by a new technique from the liver of a patient homozygous for the Z allele of the protease inhibitor locus. The material was homogenous and antigenically competent but had no protease inhibiting capacity. An interesting correlation was found between the subcellular localization and the carbohydrate composition of the Z variant from liver. Carbohydate analysis of this glycoprotein showed an absence of galactose and sialic acid, an appreciable decrease in N-acetylglucosamine, and an almost twofold increase in mannose residues. These data indicate a considerable slowdown in the processing of the oligosaccharides of liver Z variant. In spite of the absence of sialyl residues, the liver Z varant was microheterogeneous by analytical isoelectric focusing. The isoproteins of liver Z variant coincided with those of asialo M variant in the focusing field.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hercz, A -- Katona, E -- Cutz, E -- Wilson, J R -- Barton, M -- New York, N.Y. -- Science. 1978 Sep 29;201(4362):1229-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/308696" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Carbohydrate Metabolism
;
Female
;
Galactose/metabolism
;
Glycoproteins/genetics
;
Homozygote
;
Humans
;
Liver/metabolism
;
Mannose/metabolism
;
Middle Aged
;
Mutation
;
Phenotype
;
Sialic Acids/metabolism
;
alpha 1-Antitrypsin/*genetics/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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