Purification and partial amino acid sequence of annexin V from porcine gastric mucosal membranes.
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.
Baldwin
G S
GS
Ludwig Institute for Cancer Research, Royal Melbourne Hospital, Victoria, Australia.
Moritz
R L
RL
Rubira
M
M
Seet
K L
KL
Weinstock
J
J
Simpson
R J
RJ
D000595:Amino Acid Sequence; D000818:Animals; D017304:Annexin A5; D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000302:isolation & purification*; D002462:Cell Membrane / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005753:Gastric Mucosa / Q000737:chemistry* / Q000648:ultrastructure; D008969:Molecular Sequence Data; D011257:Pregnancy Proteins / Q000737:chemistry / Q000302:isolation & purification*; D016415:Sequence Alignment; D013552:Swine
D017304:Annexin A5; D002135:Calcium-Binding Proteins; D011257:Pregnancy Proteins