Donkey and horse α1B-glycoprotein: Partial characterization and new alleles

Patterson S.D., Bell K. and Shaw D.C. (1991) Donkey and horse α1B-glycoprotein: Partial characterization and new alleles. Comparative Biochemistry and Physiology -- Part B: Biochemistry and, 98 4: 523-528. doi:10.1016/0305-0491(91)90247-B


Author Patterson S.D.
Bell K.
Shaw D.C.
Title Donkey and horse α1B-glycoprotein: Partial characterization and new alleles
Journal name Comparative Biochemistry and Physiology -- Part B: Biochemistry and   Check publisher's open access policy
ISSN 0305-0491
Publication date 1991-01-01
Sub-type Article (original research)
DOI 10.1016/0305-0491(91)90247-B
Volume 98
Issue 4
Start page 523
End page 528
Total pages 6
Language eng
Subject 1303 Biochemistry
1314 Physiology
1312 Molecular Biology
Abstract 1. 1. The donkey postalbumin protein has been shown to be the equivalent of human αB-glycoprotein by protein immunoblotting and N-terminal amino acid sequence. 2. 2. The horse A1B system (already identified as the homologue of human αB-glycoprotein) and the donkey αB-glycoprotein were characterized further for terminal sialic acid content, isoelectric point, amino acid composition and affinity for the dye-ligand, Cibacron Blue F3GA (known to bind human αB-glycoprotein). 3. 3. Two new alleles in the horse A1B system were found, bringing the total number of alleles to five. No polymorphism was found in the donkey αB system. 4. 4. As expected the first 20 N-terminal residues of the donkey and horse proteins are highly conserved with only two differences being found. 5. 5. The polymorphism of the horse αB-glycoproteins may be due in part to differing numbers of terminal sialic acid residues and the higher electrophoretic mobility of the donkey αB-glycoprotein may be due in part to increased sialylation. 6. 6. The horse and donkey αB-glycoproteins exhibited differences in affinity for the dye-ligand, Cibacron Blue F3GA, with the donkey αB-glycoprotein not being bound.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import
 
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