Purification and partial amino acid sequence of annexin V from porcine gastric mucosal membranes. |
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| Authors: | G S Baldwin R L Moritz M Rubira K L Seet J Weinstock R J Simpson |
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| Affiliation: | Ludwig Institute for Cancer Research, Royal Melbourne Hospital, Victoria, Australia. |
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| 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. |
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