PURIFICATION AND N-TERMINAL CHARACTERIZATION OF CHINCHILLA-VILLIDERA ALPHA-1-ANTITRYPSIN

被引：7
|
作者：
DIVEN, WF
VIETMEIER, B
HEMPEL, J
CHAMBERS, J
机构：
[1] CHILDRENS HOSP PITTSBURGH,DEPT PEDIAT OTOLARYNGOL,PITTSBURGH,PA 15213
[2] UNIV PITTSBURGH,SCH MED,DEPT MICROBIOL BIOCHEM & MOLEC BIOL,PITTSBURGH,PA 15261
[3] UNIV TEXAS,DIV LIFE SCI,BRAIN RES LAB BIOCHEM,SAN ANTONIO,TX 78285
来源：
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1990年 / 95卷 / 01期
关键词：
D O I：
10.1016/0305-0491(90)90245-O
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
1. 1. Chinchilla, Chinchilla villidera, α-1-antitrypsin has been purified to homogeneity and partially characterized according to mol. wt, amino acid and carbohydrate composition and N-terminal amino acid sequence (30 residues). 2. 2. The mol. wt is between 52,000 and 55,000 as determined by PAGE or sedimentation equilibrium. 3. 3. The best alignment between chinchilla, human and baboon α-1-antitrypsin amino acid sequences offsets the chinchilla sequence 6 positions vs the primate structures. 4. 4. This alignment suggests potential importance of the sequence His-Glu-Gln-Glu-His at positions 11-15. 5. 5. Additionally, the segment Leu-Ala-Glu-Phe-Ala, positions 25-29, is strictly conserved. 6. 6. Shorter N-terminal sequences available for rat and rabbit α-1-antitrypsin appear to follow the offset alignment vs the primate structures. © 1989.
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页码：39 / 44
页数：6
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