GELATIN HYDROLYSATE ENZYMATIC

Assessment of Gelatinases (MMP-2 and MMP-9 by Gelatin Zymography

are multidomain proteases that contain a zinc atom in the active site and are produced in a latent inactive form (zymogen) (2 ). Acquisition of enzymatic activity requires cleavage of the inhibitory N-terminal domain (3 ). Thus, generation of the active form

Partial Enzymatic Hydrolysis of Starch to Maltodextrins on the Laboratory Scale

is virtually zero. Therefore, the dextrose equivalent is a measure of the mean average molecular mass of the starch hydrolysate. Maltodextrins are by definition nonsweet starch hydrolysates with a DE of 3 ). Starch hydrolysates with a DE above 20

A Sensitive Assay for the Enzymatic Activity of GTP Cyclohydrolase I

A chromatographic profile of neopterin. Isolation and cell culture of rat hepatocytes were performed as described (20). Hepatocytes (5 � 10 6 ) were plated onto a 90-mm gelatin-coated Petrie dish and incubated for 2 h at 37�C. Crude extracts were obtained