Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

A chondroitinase that acts upon chondroitin sulfate C and hyaluronic acid was isolated from Flavobacterium heparinum. This enzyme was seperated from constitutional chondroitinase AC and an induced chondroitinase B also present in extracts of F. heparinum previously grown in the presence of chondroitin sulfates A, B or C. The enzyme acts upon chondroitin sulfate C producing tetrasaccharide plus an unsaturated 6-sulfated disaccharide (delta Di-6S), and upon hyaluronic acid producing unsaturated nonsulfated disaccharide (delta Di-OS). Chondroitin sulfate A is also degraded producing oligosaccharides and delta Di-6S but not delta Di-4S. The chondroitinase C is also distinguished from the chondroitinases B and AC by several properties, such as effect of ions, temperature for optimal activity, and susceptibility to increasing salt concentrations. The substrate specificity of the chondroitinase C is different from that of any other chondroitinase or hyaluronidase described so far.
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PMID:Chondroitinase C from Flavobacterium heparinum. 0 3

Chondroitinase B and chondroitinase C were separated from an extract of Flavobacterium heparinum induced with chondroitin 6-sulfate by using column chromatography on hydroxylapatite. Chondroitinase C was eluted together with the activities of hyaluronidase, delta4,5glycosiduronase, and sulfatase. The latter two activities were eliminated exclusively by passing the crude chondroitinase C fraction through a phosphono-cellulose column pre-equilibrated with 0.07M sodium phosphate buffer (pH 6.8). Chondroitinase C was then purified by affinity chromatography using dermatan sulfate-bound AH-Sepharose 4B coated with the same glycosaminoglycan. Purification of the enzyme was achieved 18-fold and in 73% yield. On the other hand, the activities of delta4,5glycosiduronase and sulfatase were decreased to 50 and 60%, respectively, as compared with those in the crude chondroitinase B fraction, after passing the fraction through a column of phosphono-cellulose pre-equilibrated with 0.1M sodium phosphate buffer (pH 6.8). The remaining activities of these two enzymes were then eliminated from chondroitinase B by affinity chromatography with heparin-bound AH-Sepharose 4B coated with dermatan sulfate. In the affinity chromatography used in the present study, non-covalent coating of the glycosaminoglycan-bound (covalently) AH-Sepharose 4B with the same or another glycosaminoglycan was found to be important.
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PMID:Purification of chondroitinase B and chondroitinase C using glycosaminoglycan-bound AH-Sepharose 4B. 42 37

To generate xyloside-primed dermatan sulfate suitable for sequence analysis, skin fibroblasts were incubated with p-hydroxyphenyl-beta-D-xylopyranoside and [3H]galactose, and free [3H]glycosaminoglycan chains were isolated from the culture medium by ion exchange and gel chromatography. After 125I labelling of their reducing-terminal hydroxyphenyl groups, chains were subjected to various chemical and enzymatic degradations, both partial and complete, followed by gradient polyacrylamide gel electrophoresis and autoradiographic identification of fragments extending from the labelled reducing-end to the point of cleavage. Results of periodate oxidation-alkaline scission indicated that the xylose moiety remained unsubstituted at C-2/C-3; exhaustive treatment with chondroitin AC-I lyase afforded the fragment delta HexA-Gal-Gal-Xyl-R (R = radio-iodinated hydroxyphenyl group), and complete degradations with chondroitin ABC lyase as well as testicular hyaluronidase yielded the fragments delta HexA/HexA-GalNAc-GlcA-Gal-Gal-Xyl-R with or without sulfate on the N-acetylgalactosamine. Partial digestions with testicular hyaluronidase or chondroitin B lyase indicated that glucuronic acid was common in the first three repeats after the linkage region and that iduronic acid could occupy any position thereafter. Hence, there were no indications of a repeated, periodic appearance of the clustered GlcA-GalNAc repeats which was previously observed in proteoglycan derived dermatan sulfate [Fransson L-A, Havsmark B, Silverberg I (1990) Biochem J 269:381-8], suggesting a role for the protein part in controlling the formation of particular copolymeric features during glycosaminoglycan assembly.
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PMID:Sequence analysis of p-hydroxyphenyl-O-beta-D-xyloside initiated and radio-iodinated dermatan sulfate from skin fibroblasts. 139 65

Crude glycosaminoglycan (GAG) fraction was directly precipitated with cetylpyridinium chloride without prior dialysis of urine of orthopedic patients. The crude GAG fraction was then fractionated with trichloroacetic acid (TCA). The TCA-insoluble peptide-bound GAG fraction thus obtained was treated with alkali to eliminate the peptide moiety for enzymatic analysis. The GAG compositions of this fraction and the TCA-soluble fraction were determined by digestion with mucopolysaccharidases (chondroitinase AC, chondroitinase B, chondroitinase C, heparitinase and Streptomyces hyaluronidase). When the amount of the crude GAG fraction was small, no significant amount of the TCA-insoluble peptide-bound GAG fraction was obtained. The GAG composition of this case was also determined by the same procedures after direct alkali-treatment of the crude GAG fraction. The data indicated that the proportion of the TCA-insoluble peptide-bound GAG fraction was very small. The alkali-treated TCA-insoluble peptide-bound GAG fraction contained a larger proportion of heparan sulfate than the TCA-soluble GAG fraction. It was clearly demonstrated that the patients with Werner's syndrome and mucopolysaccharidosis I-S (Scheie) excreted large amounts of hyaluronic acid and dermatan sulfate respectively, into urines. It was indicated in most cases that major urinary GAG were chondroitin 4-sulfate, chondroitin 6-sulfate plus chondroitin and heparan sulfate, while minor ones were dermatan sulfate and hyaluronic acid. In addition, the data suggested a wide range of the degree of desulfation or urinary GAG, and the presence of significant amounts of keratan sulfate plus acidic glycopeptides in the urinary GAG fractions. The present data provided more precise information on urinary GAG from orthopedic patients than those reported previously.
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PMID:Enzymatic determination of urinary glycosaminoglycans from orthopedic patients. 640 65

A simple method for the quantitative determination of glycuronic acid-containing glycosaminoglycans (UA-GAG) is described. Sample solutions of glycosaminoglycans were digested with chondroitinase AC, chondroitinase C, chondroitinase B, heparitinases, and Streptomyces hyaluronidase, respectively, and the absorbance was read at 232 nm after digestion. The contents of 4-O-sulfated N-acetylgalactosaminyl beta (1 leads to 4)D-glucosiduronyl units (Ch-4S), 6-O-sulfated N-acetylgalactosaminyl beta (1 leads to 4)D-glucosiduronyl units (Ch-6S) plus N-acetylgalactosaminyl beta (1 leads to 4)D-glucosiduronyl units (Ch-OS), 4-O-sulfated N-acetylgalactosaminyl beta (1 leads to 4)L-idosiduronyl units (D-4S) plus N-acetylgalactosaminyl beta (1 leads to 4)L-idosiduronyl units (D-OS), heparan sulfate, and hyaluronic acid in the sample solutions were calculated from the absorbance with reference to that of the digestion products of known amounts of standard UA-GAG. The analytical data obtained with the mixtures of authentic UA-GAG were in close agreement with the theoretical values. Application of this procedure to the urinary GAG fractions from orthopedic patients gave satisfactory results.
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PMID:A simple method for the quantitation of glycuronic acid-containing glycosaminoglycans with mucopolysaccharidases. 684 97

Acidic glycoconjugates in the seminiferous tubular walls in the testes from patients with idiopathic male infertility was identified light microscopically with the sensitized high iron diamine method in combination with digestions with chondroitinase ABC, chondroitinase B or testicular hyaluronidase. Tissue specimens were obtained by testicular biopsy from 37 patients with idiopathic male infertility and 9 fertile adult males. Chondroitin sulfate A, B and C were identified in the tubular walls of oligozoospermic patients with idiopathic male infertility irrespective of the thickness of the walls. Similar results were obtained in the tubular walls of the testes from normal males. On the other hand, chondroitin sulfate B was a main acidic glycoconjugate in the tubular walls of the testes from azoospermic patients with idiopathic male infertility irrespective of the thickness of the walls. These findings suggest that the etiological factors of the impaired spermatogenesis in patients with idiopathic male infertility are not only the disturbance of nutritional transport across the seminiferous tubular walls due to peritubular thickening but the functional alterations of the tubular walls associated with changes in components of acidic glycoconjugates in the tubular walls. The pathogenesis of oligozoospermia does not seem to be similar to that of azoosspermia since components of acidic glycoconjugates in the peritubular tissues between the two types of disorders are quite different.
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PMID:[A histochemical study on the testes from patients with idiopathic male infertility: identification of acidic glycoconjugates in the seminiferous tubular walls]. 850 28

Histochemical studies were carried out in the mouse on the changes and distribution patterns of glycosaminoglycan molecular species during the separation of the lens vesicle. To obtain embryos, pregnant mice of the Jcl:ICR strain were sacrificed on day 10.5 or 11 of pregnancy. Serial frontal sections were strained with hematoxylin-eosin and sensitized high iron diamine. To identify glycosaminoglycan molecular species in tissues, an enzyme digestion (double digestion with chondroitinase B and testicular hyaluronidase) and a chemical modification (nitrous acid treatment) were performed in combination with the sensitized high iron diamine method. Before separation of the lens vesicle, chondroitin sulfate A/C and B were found in the basement membrane of the future corneal epithelium and intercellular matrices between the future corneal epithelium and lens vesicle, and chondroitin sulfate A/C was identified in the lens capsule. After separation of the lens vesicle, heparan sulfate emerged in the basement membrane of the future corneal epithelium and intercellular matrices between the future corneal epithelium and lens vesicle. These results indicate that the changes and distribution pattern of glycosaminoglycan molecular species play an important role during the separation of the lens vesicle.
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PMID:Histochemical studies of the separation of the lens vesicle in the mouse. 892 40

An electron microscopic analysis with specific histochemical stainings for acidic glycoconjugates was carried out to examine the endothelium lining blood vessels of the rat spleen. Histochemical staining performed was the postembedding high or low iron diaminethiocarbohydrazide-silver protein-physical development (HID or LID-TCH-SP-PD) method, with or without prior digestion with acidic glycoconjugate-degrading enzymes, such as heparitinase, testicular hyaluronidase, chondroitinase B and neuraminidase. The results indicated that the acidic glycoconjugates in the basal lamina of the endothelial cells lining the four types of blood vessel (central arteries, arterial capillaries, splenic sinuses and pulp veins) were heparan sulfate, chondroitin sulfate A and/or C, chondroitin sulfate B and sialic acid residues. In the endothelial cells lining the central arteries, arterial capillaries and pulp veins, the surface coat of the luminal plasma membrane included heparan sulfate, chondroitin sulfate A and/or C, chondroitin sulfate B and sialic acid residues, whereas the corresponding ultrastructure of the splenic sinuses was devoid of detectable amounts of acidic glycoconjugates. This suggests that such characteristic histochemical features of the endothelium in the four types of the splenic blood vessel can be related to the possible physiological functions of the spleen.
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PMID:Histochemical analysis of acidic glycoconjugates in the endothelium lining the splenic blood vessels in the rat. 893 40

We studied histologically the changes and distribution patterns of glycosaminoglycan molecular species during the separation of the lens vesicle in the mouse. Embryos were obtained by sacrificing pregnant mice of the Jcl: ICR strain on day 10.5 and 11 of pregnancy. Serial frontal sections were stained with hematoxylin-eosin and a sensitized high iron diamine method. To identify glycosaminoglycan molecular species in tissues, enzyme digestion (double digestions with chondroitinase B and testicular hyaluronidase) and chemical modification (nitrous acid treatment) were performed in combination with the sensitized high iron diamine method. Before separation of the lens vesicle, the glycosaminoglycan molecular species, identified in the basement membrane of the presumed corneal epithelium and intercellular matrices between the presumed corneal epithelium and lens vesicle, were chondroitin sulfate A/C and B, and those in the lens capsule were chondroitin sulfate A/C. After separation of the lens vesicle, heparan sulfate emerged in the basement membrane of the presumed corneal epithelium and intercellular matrices between the presumed corneal epithelium and lens vesicle. These results are thus taken to indicate that the changes and distribution patterns of glycosaminoglycan molecular species play an important role during separation of the lens vesicle.
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PMID:[Histochemical studies on the separation of the lens vesicle]. 902 6

Effects of a triple enzyme digestion method using glycosaminoglycans-degrading enzymes upon a diamine reaction have been tested for electron microscopic histochemical detection of glycosaminoglycans in extracellular matrix of the rat aorta. The triple enzyme digestion method consists of a sequence of chondroitinase B, testicular hyaluronidase and heparitinase. The results obtained by the present experimental and control studies indicated that dermatan sulfates, chondroitin sulfates (A and/or C) or heparan sulfates were apparently observed in various ultrastructural features of aortic extracellular matrix, such as bundle of collagen fibers and soluble matrix of interstitial space. Particularly, we found that both heparan sulfates and chondroitin sulfates (A and/or C) were detected in association with the basal lamina of smooth muscle cells and the external surface of elastic lamina, and in the latter heparan sulfates were frequently recognized as a mass, whereas chondroitin sulfates (A and/or C) were found intermittently along the external surface of elastic lamina. This suggests that the triple enzyme digestion method which combines the glycosaminoglycans-degrading enzymes with the diamine reaction can be postulated to represent efficient and useful technique for precise electron microscopic histochemical detection of the glycosaminoglycans in the extracellular matrix of the rat aorta.
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PMID:Effects of a triple enzyme digestion method on a diamine reaction for glycosaminoglycans of the rat aorta in electron microscopy. 985 95


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