Unique amino terminal structure of rat little gastrin.
Peptides
; 2(4): 453-8, 1981.
Article
em En
| MEDLINE
| ID: mdl-7329823
ABSTRACT
The heptadecapeptide form of rat gastrin was purified by a combination of DEAE cellulose, Sephadex G50 affinity, and high performance liquid chromatography. An amino terminal pyroglutamyl blocking group was removed by incubation with PCA peptidase. Amino acid analysis before and after the unblocking reaction revealed the presence of one additional residue of arginine and proline compared with porcine gastrin. Microsequencing analysis of the unblocked peptide revealed that the sequence of the remaining hexadecapeptide was RPPMEEEEEAYGWMDF. The corresponding sequence of porcine gastrin is GPWMEEEEEAYGWMDF amide. The presence of carboxyl-terminal amide group in rat gastrin is strongly supported by complete immunoreactivity with antibodies specific for amidated C-terminal sequences of mammalian gastrins. The Arg and Pro substitutions in the amino terminal region can explain poor crossreactivity of rat gastrin with antibodies specific for the amino-terminal portion of porcine or human gastrin and its more basic chromatography pattern on ion exchange resins.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Antro Pilórico
/
Gastrinas
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Peptides
Ano de publicação:
1981
Tipo de documento:
Article