Isolation and characterization of rabbit gastrin.
The heptadecapeptide form the rabbit gastrin was extracted from 16 rabbit antra and purified by a combination of DEAE Sephadex, C-18 SEP PAK cartridges, fast performance liquid chromatography (FPLC) and reverse phase high pressure liquid chromatography (HPLC) steps. After the HPLC purification, a sharp, single peak of gastrin-like immunoreactivity was detected that had the same absorption to immunoreactivity ratio as human gastrin. An amino terminal pyrrolidone carboxylic acid blocking group was removed by incubation with pyrrolidone carboxylic peptidase. The amino acid analysis, microsequence analysis and mass spectrometry all confirmed the structure of rabbit gastrin being pQGPWLQEEEEAYGWMDFamide. This sequence is identical to human gastrin-17 except for glutamine in position 6 which replaces glutamate in human gastrin. Both sulfated and unsulfated rabbit gastrin-17 were characterized by mass spectrometry.
Jiang
R
R
First Teaching Hospital of China Medical University, Peoples Republic of China.
Huebner
V D
VD
Lee
T D
TD
Chew
P
P
Ho
F J
FJ
Shively
J E
JE
Walsh
J H
JH
Reeve
J R
JR
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002853:Chromatography, Liquid; D005755:Gastrins / Q000302:isolation & purification*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D011706:Pyloric Antrum; D011817:Rabbits; D011863:Radioimmunoassay
D000596:Amino Acids; D005755:Gastrins