Separation of porcine pepsinogen A and progastricsin. Sequencing of the first 73 amino acid residues in progastricsin.
Porcine pepsinogen A (EC 3.4.23.1) and progastricsin (EC 3.4.23.3) have been separated by chromatography on DEAE-cellulose followed by chromatography on DEAE-Sepharose. Agar gel electrophoresis at pH 6.0 showed the presence of three components of pepsinogen A and two of progastricsin. During activation at pH 2 a segment of 43 amino acid residues (the prosegment peptide) is cleaved from the N-terminus of progastricsin. The sequence of this was determined; in addition, the first 30 residues of gastricsin were sequenced. The sequence of the first 73 amino acid residues of progastricsin shows an overall identity with progastricsins from man, monkey and rat of 67%. The overall identity with other zymogens for gastric proteinases is 27%. The highly conserved Lys36p (pig pepsinogen A numbering) is changed to Arg in porcine progastricsin.
Foltmann
B
B
Institute of Biochemical Genetics, University of Copenhagen, Denmark.
Drøhse
H B
HB
Nielsen
P K
PK
James
M N
MN
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004587:Electrophoresis, Agar Gel; D004789:Enzyme Activation; D005753:Gastric Mucosa / Q000201:enzymology*; D007122:Immunoelectrophoresis; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010435:Pepsinogens / Q000737:chemistry / Q000302:isolation & purification*; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D013552:Swine
D010435:Pepsinogens