Journal of the American Chemical Society p. 7299 - 7306 (1982)
Update date:2022-08-05
Topics:
Melhado, L. Lee
Peltz, Stuart W.
Leytus, Steven P.
Mangel, Walter F.
Two active-site titrants of serine proteases, fluorescein mono-p-guanidinobenzoate hydrochloride (FMGB*HCl) and fluorescein di-p-guanidinobenzoate dihydrochloride (FDGB*2HCl), have been synthesized, purified, and chemically and enzymatically characterized.Electronic absorbtion and fluorescence emission spectra, fluorescence lifetimes and quantum yields, solubilities, and rates of spontaneous hydrolysis at pH 7-10 are reported.Macroscopic and microscopic kinetic constants for interaction of FMGB*HCl with trypsin, urokinase, plasmin, and trombin have been determined.FMGB*HCl, which rapidly releases fluorescein upon formation of a stable acyl-enzyme intermediate with tripsin and other trypsin-like enzymes, is the most sensitive active-site titrant for serine proteases yet described.
View MoreContact:+86-22-26358246
Address:601-4-20, Fujiayuan, Tiantai Road, Hebei District, Tianjin, China
Contact:+86+21-58956006 15800617331
Address:402 Room, 150# Cailun Road, Zhangjiang high tech park, Shanghai
SPRING CHEMICAL INDUSTRY CO.,LTD
Contact:86-187-66672125
Address:linchi industry park.zouping
He Bei Shun Er Chemical Co., LTD.
Contact:86-0311-86996932/86860168
Address:No 18,North street
Hangzhou Ledun Technology Co.,Ltd.
Contact:86-571-18767088918
Address:No.6 street,XiaSha,Hangzhou,China.
Doi:10.1248/cpb.30.2586
(1982)Doi:10.1021/ja043898r
(2005)Doi:10.1016/j.tet.2006.06.083
(2006)Doi:10.1021/jm00357a026
(1983)Doi:10.1007/s11176-005-0097-1
(2004)Doi:10.1248/cpb.30.3054
(1982)