Potato tuber protein proteinase inhibitors belonging to the Kunitz soybean inhibitor family.
Biochemistry (Mosc)
; 62(12): 1367-74, 1997 Dec.
Article
en En
| MEDLINE
| ID: mdl-9481870
ABSTRACT
Three protein inhibitors of proteolytic enzymes with molecular weights 21, 22, and 23 kD were isolated from potato tubers (Solanum tuberosum L.) by ammonium sulfate precipitation followed by gel and ion-exchange chromatography. The 21- and 22-kD proteins were shown to be serine proteinase inhibitors with different specificities. The 21-kD protein inhibits human leucocyte elastase and trypsin effectively, but it is less effective towards chymotrypsin. The 22-kD protein is an inhibitor of cysteine proteinases and suppresses the activities of papain, ficin, and bromelain with the same affinities. None of the isolated proteins inhibit subtilisin, pepsin, or cathepsin D. The 21-kD protein consists of two disulfide-linked polypeptide chains with molecular weights of 16.5 +/- 1 kD and 4.5 +/- 1 kD. The 22-kD and 23-kD proteins have a single polypeptide chain. The N-terminal 22-25 amino acid sequences of these three proteins were determined. These sequences have significant homology to other plant inhibitors from the Kunitz soybean inhibitor superfamily.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Solanum tuberosum
/
Inhibidor de la Tripsina de Soja de Kunitz
Límite:
Humans
Idioma:
En
Revista:
Biochemistry (Mosc)
Año:
1997
Tipo del documento:
Article
País de afiliación:
Rusia