Cationic proteins from human neutrophil granulocytes. Evidence for their chymotrypsin-like properties.
Biochim Biophys Acta
; 379(2): 606-17, 1975 Feb 27.
Article
en En
| MEDLINE
| ID: mdl-235318
ABSTRACT
Three cationic proteins from the granules of human neutrophil granulocytes were obtained in a high degree of purity be means of affinity chromatography on 4-phenylbutylamine-Sepharose. Together with lysozyme, the three cationic proteins exhibit the highest electrophoretic mobility toward the cathode in acrylamide gels at moderately acid pH, among the granule constituents that are solubilized in 0.1 M phosphate buffer, pH 7.0, containing 1 M NaCl. The three cationic proteins represent a group of "neutral proteases" distinct from elastase and collagenase. They hydrolyze casein, azocasein and the chymotrypsin substrate N-acetyl-L-tyrosine ethyl ester. Optimal activity is found at pH 7.4-7;5. The enzymes are inhibited by the specific chymotrypsin inhibitor N-tosyl-L-phenylalanylchloromethane and by the naturally occurring inhibitors alpha-antichymotrypsin, alpha-1-antitrypsin, as well as by the trypsin inhibitors from soy beans and limabeans.
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Banco de datos:
MEDLINE
Asunto principal:
Proteínas Sanguíneas
/
Quimotripsina
/
Granulocitos
/
Leucocitos
/
Neutrófilos
Límite:
Humans
Idioma:
En
Año:
1975
Tipo del documento:
Article