trypsinogen

Aprotinin (Traskolan) 是一种广谱丝氨酸蛋白酶 (BPTI) 抑制剂，可抑制多种不同酯酶和蛋白酶的活性。Aprotinin 是一种抗纤溶剂，用于减少复杂手术中的出血。

Chymotrypsinogen 是Chymotrypsin 的无活性前体。Chymotrypsinogen 是一种由胰腺产生的丝氨酸蛋白酶 (serine protease)。

L-Cystine (Cystine Acid) 是一种从半胱氨酸氨基酸硫醇侧链氧化获得的含硫衍生物。它起到抗氧化剂的作用，保护组织免受辐射和污染，减缓衰老过程。它还有助于蛋白质合成。

MBD, a novel fluorescent probe (7-(p-Methoxybenzylamino)-4-nitrobenz-2,1,3-oxadiazole), is utilized to study the conformation of protein and nucleoprotein. Its application is extended to bacterial ribosomes, as well as bovine trypsinogen and trypsin. MBD exhibits significant fluorescence when it binds to the hydrophobic region of macromolecules [1][2].

Enteropeptidase fluorogenic substrate is a substrate for enteropeptidase that contains a 7-amino-4-trifluoromethylcoumarin (AFC) moiety. Enteropeptidase is a serine protease expressed in the proximal small intestine of higher animals that converts inactive trypsinogen to active trypsin by endoproteolytic cleavage. Enteropeptidase recognizes the highly specific amino acid sequence DDDDK on the fluorogenic substrate and cleaves after the lysine residue, releasing the AFC moiety. Enteropeptidase activity is quantified by fluorescent detection of AFC, which displays excitation emission spectra of 380 500 nm.

Enteropeptidase fluorogenic substrate is a substrate for enteropeptidase that contains a 7-amino-4-trifluoromethylcoumarin (AFC) moiety. Enteropeptidase is a serine protease expressed in the proximal small intestine of higher animals that converts inactive trypsinogen to active trypsin by endoproteolytic cleavage.1,2Enteropeptidase recognizes the highly specific amino acid sequence DDDDK on the fluorogenic substrate and cleaves after the lysine residue, releasing the AFC moiety. Enteropeptidase activity is quantified by fluorescent detection of AFC, which displays excitation/emission spectra of 380/500 nm.3