Isolation and amino acid sequence of two trypsin isoinhibitors from duck pancreas.
DPTI II and DPTI IV, two trypsin inhibitors from duck pancreas, have been isolated by affinity chromatography on immobilized anhydrotrypsin, anion exchange and RP-HPLC. The complete amino acid sequence of both inhibitors was determined after reductive carboxymethylation and digestion with Staphylococcus aureus V8 protease or trypsin. The inhibitors were each found to be a single polypeptide chain comprised of 69 amino acid residues and their molecular masses were estimated at 7687 Da for DPTI II and 7668 Da for DPTI IV. The only difference in amino acid sequence between the two inhibitors is the replacement of Arg for His residue in the C-terminal position of DPTI IV.
Wilimowska-Pelc
A
A
Institute of Biochemistry and Molecular Biology, University of Wrocław, Poland. anna@bf.uni.wroc.pl
Olczak
M
M
Olichwier
Z
Z
Gładysz
M
M
Wilusz
T
T
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D004372:Ducks; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010179:Pancreas / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D020033:Protein Isoforms; D020539:Sequence Analysis, Protein; D012697:Serine Endopeptidases / Q000378:metabolism; D013045:Species Specificity; D014361:Trypsin Inhibitors / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology
D000596:Amino Acids; D010455:Peptides; D020033:Protein Isoforms; D014361:Trypsin Inhibitors; C403842:trypsin inhibitor, duck pancreas; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase