Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.2.2.7 (heparinase)
 1,270 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Histochemical localization of the estrogen-induced sulfated glycoproteins was made in the estrogen-treated rabbit uterus. Biochemical studies by a group of Endo et al, affirmed these particular glycoproteins were PAS-positive and metachromatic as stained with TB. No sign of digestion, however, has been detected in a series of tests with alpha-amylase, testicular hyaluronidase, streptomyces hyaluronidase, chondroitinase AC and chondroitinase ABC, and heparinase. The apical portions of the epithelial and glandular cells, obviously expanded by the estrogen treatment, display strong beta-metachromasia with TB (pH 4.0), saliva-resistant PAS-positive reactions, and also alcianophilia with AB (pH 2.5). These reactions are not reduced after the treatment with the enzymes above-mentioned. Meanwhile, in the stromal matrix, the same enzymes give an influence to diminish the reactions to various extent. Our results suggest that the estrogen-induced sulfated glycoprotein is definitely localized in the apical portions of the epithelial and glandular cells. The identity is emphasized between the substance that is elucidated in the histochemical sections and the sulfated glycoproteins that have been specified solely by means of biochemical assays.
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PMID:Histochemical localization of estrogen induced sulfated glycoprotein in rabbit uterus. 5 8

Dextran sulfate sodium (DSS) is a strong negatively charged heparin-like polysaccharide and has anti-immunodeficiency virus, anti-carcinogenesis, or occasionally tumor-promotion effects. The biological metabolism of DSS, however, remains unclear. In a previous study, we reported a novel method for the separation and quantification of DSS, using fluorometric labeling with 2-aminopyridine and a combination of size-exclusion and reverse phase high-performance liquid chromatography. In the present study, we have applied this method for analyses of in vitro chemical or enzymatic depolymerization of pyridylamino-DSS (PA-DSS). PA-DSS was depolymerized by specific enzymes such as alpha-amylase and alpha-glycosidase, but not by dextranase or heparinase. Unknown enzymes derived from cultured intestinal cells also strongly depolymerized PA-DSS as did alkaline substances. On the other hand, we have established a novel detection system using a post-column reaction. This method utilizes the spectrophotometrically metachromatic reaction of toluidine blue solution with DSS. This novel detection system may be specific and may potentially provide useful information in the analyses of sulfated polysaccharides, which are present in environmental and biological materials.
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PMID:The analysis of pyridylamino-dextran sulfate oligomers by high-performance liquid chromatography and a novel detection system for sulfated polysaccharides. 1525 3