Isolation and characterisation of porcine sorbin.
Sorbin has been isolated from extracts of porcine upper intestine, and the biological activity in absorbing water and electrolytes utilized to monitor the purification procedure. Pure sorbin was obtained in a yield of about 1 mg/Mg boiled intestine. The protein chain has 153 amino acid residues and the primary structure was determined by analyses of CNBr-cleaved fragments and four enzymatic digests. The protein has a free N-terminal Met and an amidated C-terminal Ala. No structural similarity was observed with other known proteins in data bases, but several segments have special properties and the C-terminal half is rich in Pro and Arg.
INSERM U 45, Hôpital E Herriot, Lyon, France.
M
M
Vagne-Descroix
D
D
Pansu
H
H
Jörnvall
M
M
Carlquist
H
H
Guignard
G
G
Jourdan
A
A
Desvigne
M
M
Collinet
C
C
Caillet
V
V
Mutt
D000042:Absorption; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003488:Cyanogen Bromide; D005704:Gallbladder / Q000187:drug effects / Q000378:metabolism; D006168:Guinea Pigs; D007422:Intestines / Q000737:chemistry*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D013552:Swine; D014867:Water / Q000378:metabolism
D000596:Amino Acids; D010446:Peptide Fragments; D010455:Peptides; D014867:Water; C071218:sorbin peptide; D003488:Cyanogen Bromide