The amino acid sequence of a novel inhibitor of cathepsin D from potato.
The amino acid sequence of a cathepsin D inhibitor isolated from potato is described. It was determined by analysis of peptides generated by use of the glycine-specific proteinase PPIV. The order of the peptides was established by examination of tryptic peptides derived from the two cyanogen bromide peptides. The inhibitor comprises 187 amino acid residues, and has a calculated Mr of 20,450.
Ritonja
A
A
Department of Biochemistry, Jozef Stefan Institute, Ljubljana, Yugoslavia.
Krizaj
I
I
Mesko
P
P
Kopitar
M
M
Lucovnik
P
P
Strukelj
B
B
Pungercar
J
J
Buttle
D J
DJ
Barrett
A J
AJ
Turk
V
V
D000595:Amino Acid Sequence; D002402:Cathepsin D / Q000037:antagonists & inhibitors; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D008969:Molecular Sequence Data; D011480:Protease Inhibitors / Q000032:analysis*; D011198:Solanum tuberosum / Q000201:enzymology*
D011480:Protease Inhibitors; D002402:Cathepsin D