Hyaluronic acid hydrolysis, enzymic

The PL-catechin conjugate showed greatly amplified concentration-dependent inhibition activity against bacterial collagenase (ChC) on the basis of the catechin unit, which is considered to be due to effective multivalent interaction between ChC and the catechin unit in the conjugate. The kinetic study suggests that this conjugate is a mixed-type inhibitor for ChC. Hyaluronidase is an enzyme which catalyzes hydrolysis of hyaluronic acid and is often involved in a number... 

The structure of hyaluronic acid is now well established. Acidic hydrolysis yields the constituent disaccharide, hyalobiouronic acid, whose structure was shown to be 2-amino-2-deoxy-3-0-(P-D-glucopyranosylu-ronic acid)-D-glucose by degradative studies (W3) and, more recently, by constitutional syntheses (J7, Tl). The hexosaminidic linkage has been shown to have a pi- 4 configuration by enzyme (W4) and methylation (Hll) studies, so that hyaluronic acid may be assigned structure (1). 

Disaccharides from glycosanunoglycans. - Unsaturated disaccharides released by enzymic hydrolysis of chondroitin sulphate have been separated on a primary amino-containing gel column, those from hyaluronic acid, chondroitin sulphate and dermatan sulphate by reversed-phase h.p.l.c. on an amido-phase as their dansyl hydrazone derivatives with chemiluminescence detection," and those from dermatan sulphate and heparin by ion-pair reversed-phase microbore h.p.Lc. coupled with ion-spray m.s. for use in monitoring their presence in patients treated vrith these polysaccharides intravenously. ... 

Values for Km and have been determined for the degradation of chondroitin 4- and 6-sulphates, chondroitin 4-sulphate proteoglycan, dermatan sulphate, and hyaluronic acid by a chondroitin sulphate lyase ABC obtained from Proteus vulgaris. The hydrolysis of chondroitin 4-sulphate by the enzyme was inhibited by hyaluronic acid, but not by keratan sulphate. The findings were discussed in connection with the use of chondroitin sulphate lyase ABC as a reagent for the degradation of tissue glycosaminoglycans. 

A new semimicro assay for hyaluronidase has used [ H]hyaluronic acid as a substrate. After enzymic hydrolysis of the substrate, cetylpyridinium chloride is added to the hydrolysate to precipitate any unreacted substrate, and the soluble [ H]oligosaccharides are then determined by scintillation counting. 

For the polysaccharide synthesis, enzymatic polymerization has been developed as a new in vitro synthesis method of natural and unnatural polysaccharides having complicated structures.The method utilizes a hydrolysis enzyme to catalyze the bond formation for the polymer construction, a reverse direction of the hydrolysis to cleave the bond. This catalysis is due to the enzymatic characteristics, where enzymes catalyze the reverse reaction involving a common intermediate in both forward and backward reactions. In nature, there are many polysaccharides having N-acetyl groups called mucopolysaccharides such as chitin, hyaluronic acid (HA), and chondroitin (Ch). 

The enzyme is frequently referred to as the spreading factor because hydrolysis of hyaluronic acid facilitates toxin diffusion into the tissues of the victim. Hyaluronidase itself can be- separated from the toxic fraction, hence is not a main factor. Despite the importance of this enzyme in snake venom action, it has not been isolated in pure form. 

Hyaluronidase Hydrolysis of 1,4 bonds between 2-acetamido-2-deoxy-/i-D-glucose and D-glucuronic acid in hyaluronic add. Enzyme also hydrolyzes 1,4-bonds in some other polysaccharides containing sulfate groups Heart attack Spectrophotometry One unit produces absorbance equivalent to 1.0 pg of glucuronic acid per hour from hyaluronic add, using 3,5-dinitrosali(ylic acid to develop the color. 

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