PURIFICATION AND PARTIAL AMINO-ACID-SEQUENCE OF ANNEXIN-V FROM PORCINE GASTRIC-MUCOSAL MEMBRANES
Details
Publication Year 1991, Volume 100, Issue #4, Page 661-665
Journal Title
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
Publication Type
Journal Article
Abstract
1. Annexin V has been purified from Triton X-100 extracts of porcine gastric mucosal membranes by a combination of chromatography on concanavalin A-Sepharose and DEAE-Sepharose, and preparative gel electrophoresis. 2. No N-terminal amino acid sequence was detected. 3. The sequences of 11 tryptic peptides were determined, amounting to a total of 121 amino acids, or 38% of the molecule. 4. When the peptides were compared with the cDNA-derived sequence of human annexin V, only three substitutions were observed. 5. Human and porcine annexin V are 97% homologous within the sequenced regions.
Publisher
PERGAMON-ELSEVIER SCIENCE LTD
Keywords
PLACENTAL ANTICOAGULANT PROTEIN; PHOSPHOLIPID-BINDING PROTEIN; CALCIUM-CHANNEL ACTIVITY; EPIDERMAL GROWTH-FACTOR; LIPOCORTIN; CDNA; HOMOLOGY; EXPRESSION; CALPACTIN; CRYSTAL
Rights Notice
Refer to copyright notice on published article.


Creation Date: 1991-01-01 12:00:00
Last Modified: 0001-01-01 12:00:00
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