PURIFICATION AND PARTIAL AMINO-ACID-SEQUENCE OF ANNEXIN-V FROM PORCINE GASTRIC-MUCOSAL MEMBRANES

Author(s): Baldwin, GS; Moritz, RL; RUBIRA, M; SEET, KL; Weinstock, J; Simpson, RJ;
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
Publisher's Version: https://doi.org/10.1016/0305-0491(91)90271-E
Terms of Use/Rights Notice: Refer to copyright notice on published article.

Creation Date: 1991-01-01 12:00:00