绒鼠α-1-抗胰蛋白酶的纯化及N端特性分析

Purification and N-terminal characterization of Chinchilla villidera alpha-1-antitrypsin.

Diven W F, Vietmeier B, Hempel J, Chambers J

Department of Pathology, School of Medicine, University of Pittsburgh, PA 15261.

Comp Biochem Physiol B. 1990;95(1):39-44. doi: 10.1016/0305-0491(90)90245-o.

Abstract

Chinchilla, Chinchilla villidera, alpha-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. The mol. wt is between 52,000 and 55,000 as determined by PAGE or sedimentation equilibrium. 3. The best alignment between chinchilla, human and baboon alpha-1-antitrypsin amino acid sequences offsets the chinchilla sequence 6 positions vs the primate structures. 4. This alignment suggests potential importance of the sequence His-Glu-Gln-Glu-His at positions 11-15. 5. Additionally, the segment Leu-Ala-Glu-Phe-Ala, positions 25-29, is strictly conserved. 6. Shorter N-terminal sequences available for rat and rabbit alpha-1-antitrypsin appear to follow the offset alignment vs the primate structures.

摘要

已将毛丝鼠（Chinchilla villidera）的α-1-抗胰蛋白酶纯化至同质，并根据分子量、氨基酸和碳水化合物组成以及N端氨基酸序列（30个残基）进行了部分表征。2. 通过PAGE或沉降平衡测定，其分子量在52,000至55,000之间。3. 毛丝鼠、人类和狒狒α-1-抗胰蛋白酶氨基酸序列之间的最佳比对使毛丝鼠序列相对于灵长类结构偏移了6个位置。4. 这种比对表明第11至15位的His-Glu-Gln-Glu-His序列具有潜在重要性。5. 此外，第25至29位的Leu-Ala-Glu-Phe-Ala片段严格保守。6. 可用于大鼠和兔α-1-抗胰蛋白酶的较短N端序列似乎遵循相对于灵长类结构的偏移比对。