Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Chondroitin sulfate fractions were isolated from different animal cartilages, including whale, cattle, sheep, ray and shark, by Dowex 1 chromatography followed by ethanol fractionation. Although each preparation showed a single spot when electrophoresed on cellulose acetate, both 4- and 6-sulfated disaccharides were present in chondroitinase digests of each. In particular, the main fraction of bovine tracheal chondroitin sulfate (SO4/Ga1N = 1) gave both the disaccharides in nearly equal amounts, and its IR spectrum showed absorption bands at 820 and 850 cm-1. This fraction yielded three types of tetrasaccharides after digestion with testicular hyaluronidase. Structural studies on these tetrasaccharides, using P. vulgaris chondro-4-sulfatase followed by chondroitinase, showed that one of them is a hybrid consisting of the 4- and 6-sulfated residues. In the light of these facts, a nomenclature for chondroitin sulfates is discussed.
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PMID:Microheterogeneity of chondroitin sulfates from various cartilages. 12 31

The dodecasaccharide obtained by treating dermatan sulfate with testicular hyaluronidase, chondroitinase AC, and beta-glucuronidase was incubated with diluted, normal human serum at pH 4.5 or 7.0 followed by chondro-4-sulfatase at pH 7.0. Analyses of the reaction products indicate release of hexosamine but not further degradation of the substrate. It is concluded that normal human serum possesses an exo-beta-N-acetylhexosaminidase active on dermatan sulfate.
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PMID:Beta-N-acetylhexosaminidase active on dermatan sulfate. 109 49

Salt extracts of the extracellular matrix (ECM) that is produced by vascular and capillary endothelial cells contain mitogens that are indistinguishable from basic and acidic fibroblast growth factors (FGFs). The biological activity found in these extracts is retained by heparin-Sepharose affinity columns and elutes with salt concentrations similar to those required to elute FGFs (i.e. 1.1 - 2M NaCl). Antisera raised against synthetic fragments of basic and acidic FGF crossreact with the ECM-derived mitogens. Radioiodinated basic FGF binds to the ECM formed by both vascular and capillary endothelial cells, a result that is consistent with the observation that FGF-like mitogens are found on the ECM. The binding of FGF to the ECM is negligible when the ECM has been pretreated with heparinase or heparitinase suggesting that the mitogen is interacting with a heparin-like glycosaminoglycan in the ECM. The digestion of the ECM with several grades of hyaluronidase, chondroitinase or chondro-4-sulfatase or chondro-6-sulfatase has little or no effect on 125I-FGF binding to the ECM. In view of the fact that many, if not all cells, produce heparan sulfates and that these glycosaminoglycans are associated with the external surface of the cell and the ECM, a model is proposed suggesting that the neovascular response induced by tumours and some normal tissues may be mediated at least in part, by the initial release of heparinase-like enzymes rather than angiogenic factors (FGFs) per se. The release of these enzymes would effectively mobilize a secondary local release of FGF from the ECM which then induces a proliferative response.
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PMID:Fibroblast growth factors are present in the extracellular matrix produced by endothelial cells in vitro: implications for a role of heparinase-like enzymes in the neovascular response. 243 94

The murine monoclonal antibody (MAb) designated DF3 has defined a high m.w. antigen detectable in human breast carcinomas and in human milk. DF3 antigen is detectable on apical borders of secretory mammary epithelial cells and in the cytosol of less differentiated malignant cells. DF3 antigen expression has been shown to correlate with the degree of human breast tumor differentiation, and the detection of a cross-reactive species in human milk has suggested that DF3 antigen might be useful as a biochemical marker of differentiated mammary epithelial cells. To further characterize DF3 antigen, we have developed an approach to purify the cross-reactive species by using gel filtration and antibody affinity chromatography. The affinity column-purified DF3 antigen was absorbed by wheat germ agglutinin and peanut agglutinin, but not by concanavalin A or lentil lectin. In contrast, wheat germ agglutinin inhibited MAb DF3 reactivity with the purified antigen, whereas there was little, if any, inhibition when using peanut agglutinin. These findings are thus consistent with the involvement of terminal N-acetyl-D-neuraminic acid and/or N-acetylglucosamine residues in the antigenic site. DF3 antigenicity was also sensitive to neuraminidase, but not chondroitinase ABC, chondroitinase AC, chondroitin-4-sulfatase, or hyaluronidase. Furthermore, DF3 antigen was sensitive to Pronase, subtilisin BPN', and alpha-chymotrypsin. The presence of O-glycosidic linkages between carbohydrate and protein in the DF3 antigenic site was further supported by the presence of NaBH4-sensitive sites. Together, these results suggest that sialyl oligosaccharides present on a peptide backbone are required for maintaining DF3 antigenicity. Similar findings have been demonstrated for DF3 antigen purified from both human milk and breast cancer effusions. However, the DF3 antigen in human milk consisted of a single high m.w. species, whereas the tumor-associated antigen consisted of two distinct glycoproteins with m.w. of 330,000 and 450,000. These findings may be relevant to the recent demonstration that distinct high m.w. DF3 antigens are elevated in the circulation of patients with breast carcinoma.
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PMID:Purification and characterization of a high molecular weight glycoprotein detectable in human milk and breast carcinomas. 404 99