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)

Bull seminal-plasma hyaluronidase was purified 180-fold by chromatography on concanvalin A-Sepharose, heparin Sepharose, Sephadex G-200 and Sephacryl S-200. With hyaluronic acid as the substrate, the specific activity and turnover number of purified hyaluronidase were 3.63 mumol/min per mg (104000 National Formulary units/mg of protein) and 214 min-1 (mol of product formed/mol of enzyme per min) respectively. Polyacrylamide-gel electrophoresis indicated that the purified enzyme migrated as a single band on 7.5 and 10% (w/v) gels at pH 4.3 and 5.3. Bull seminal-plasma hyaluronidase was markedly inhibited by hydroxylamine, phenylhydrazine and semicarbazide. Purified hyaluronidase (1.25 munits; 1 unit = 1 mumol of N-acetylglucosamine liberated/min at 37 degrees C) dispersed the cumulus clot of rabbit ova in 1 h at 22 degrees C.
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PMID:Heparin-sepharose affinity chromatography for purification of bull seminal-plasma hyaluronidase. 54 29

Several substances have been claimed to be effective in reducing the area of necrosis in acute myocardial infarction. The effects of a highly purified hyaluronidase preparation (Hyalas) on experimental myocardial infarction in the rat have been evaluated in this study. In the first series, one group of rats was treated with hyaluronidase 1 500-2 000 IU/kg injected intravenously 2, 4, 18, 24, 28 and 42 hours after induction of infarction by coronary artery occlusion. Another group was treated with NaCl solution. The infarction size was evaluated by serum lactate dehydrogenase and weight of infarcted myocardium. In a second series, the substances were administered immediately after the occlusion. In this experiment, the infarction size was estimated by planimetry. The percentage of salvaged myocardium in the hyaluronidase-treated groups was within the range of 20%. It seems reasonable to suggest that the use of highly purified hyaluronidase may be of clinical value for reduction of the myocardial infarction size.
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PMID:The effects of a highly purified hyaluronidase preparation on experimental myocardial infarction in the rat. 649 78

The sonication method produced a quantitatively higher release of buffalo sperm hyaluronidase than the freeze-thaw technique. The released enzyme constituted 10 p. 100 of the total enzymatic activity of the fresh semen. Seminal plasma hyaluronidase activity was not correlated with the motility score of the semen sample. Unlike cattle semen, the seminal plasma enzyme level in buffalo semen stored at 37 degrees C showed a sharp rise, whereas samples stored at 0 degrees C evidenced negligible enzyme leakage. Dilution of semen in citric acid whey (CAW) at 5 or 37 degrees C significantly prevented the enzyme from leaking into the plasma, although more enzyme was released in extended semen when it was exposed to cold treatments. The enzyme was quite stable in both the seminal plasma and the acrosomal preparations during storage when stored at 5 degrees C for prolonged periods.
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PMID:On the leakage of acrosomal hyaluronidase from the spermatozoa of the buffalo (Bubalus bubalis). 734 30

Hyaluronidase, a lysosomal endoglycosidase mediating hyaluronan (hyaluronic acid) turn-over, is thought to be important in many normal developmental and certain pathologic processes. Previous assays of serum hyaluronidase are limited with respect to their applicability for routine clinical chemistry or clinical biochemical genetics applications. We describe a new assay of human serum or plasma hyaluronidase activity based on the determination of released N-acetylglucosamine reducing termini that allows the analysis of the enzyme with small, easily obtained sample volumes. Using 10 microliters of serum or plasma, sodium formate buffer and human umbilical cord hyaluronan as substrate, we found a pH optimum of 3.9 and a K(m) and Vmax of 114 mg/l and 5102 mU/l, respectively. In addition, the assay has excellent linearity, precision and reproducibility.
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PMID:Human serum hyaluronidase: characterization of a clinical assay. 864 8

Hyaluronidase was purified from human plasma using Triton X-114 phase extractions and ion-exchange chromatography. Monoclonal antibodies generated against the purified protein by a novel screening assay were utilized to isolate homogeneous enzyme for microsequencing. The amino acid sequences obtained matched a cDNA in the Expressed Sequence Tag database which, with 5'-RACE-PCR, was used to clone the plasma hyaluronidase gene, termed Hyal-1. Hyal-1 codes for a protein of 435 amino acids that is over 40% identical to PH-20, a sperm-specific hyaluronidase. Unlike PH-20, which is only expressed in testis, transcripts of Hyal-1 were found in multiple tissues. Hyal-1 stably expressed in human embryonic kidney cells resulted in a 3,000 fold increase of secreted immunoreactive hyaluronidase activity that was biochemically indistinguishable from human plasma hyaluronidase. By immunological, molecular and biochemical criteria, we conclude that Hyal-1 is the predominant hyaluronidase found in human plasma.
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PMID:Purification, cloning, and expression of human plasma hyaluronidase. 922 16

A nearly pathognomonic finding of the lysosomal storage disorders mucolipidoses II and III is the marked increase of plasma lysosomal enzyme activities. The genetic lesion in ML II and III causes defective function of the enzyme UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase. Defective function of this enzyme results in deficient phosphorylation of lysosomal enzyme asparagine-linked oligosaccharides and a consequent misrouting of many newly synthesized lysosomal enzymes. These enzymes are secreted from cells instead of being targeted to lysosomes, with resultant marked elevations of multiple lysosomal enzyme activities in plasma. We report here that plasma hyaluronidase activity, an endoglycosidase of presumably lysosomal origin, is not increased in the plasma from individuals with mucolipidoses II and III, unlike most lysosomal enzymes. Our data suggest the possibility that hyaluronidase is not targeted to lysosomes by a lysosomal enzyme phosphosmannosyl recognition mechanism. Alternatively, hyaluronidase activity may not be present in the cell type(s) responsible for the lysosomal enzyme hypersecretion in mucolipidoses II and III which, along with its deficiency in fibroblasts and leukocytes, would constitute an unusual tissue distribution of activity for a soluble lysosomal enzyme.
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PMID:Plasma hyaluronidase activity in mucolipidoses II and III: marked differences from other lysosomal enzymes. 924 Jul 45

A sensitive, rapid microtiter-based assay for hyaluronidase activity is described that does not require highly specialized biological reagents, as required heretofore. The free carboxyl groups of hyaluronan are biotinylated in a one-step reaction using biotin-hydrazide. This substrate is then covalently coupled to a 96-well microtiter plate. At the completion of the enzyme reaction, residual substrate is detected with an avidin-peroxidase reaction that can be read in a standard ELISA plate reader. Because the substrate is covalently bound to the microtiter plate, artifacts such as pH-dependent displacement of the biotinylated substrate do not occur. The sensitivity permits rapid measurement of hyaluronidase activity from cultured cells and biological samples with an interassay variation of less than 5%. Using this new assay, we measured the distribution profile of plasma hyaluronidase levels in normal human sera. A 1-microl sample of plasma was sufficient for assays in triplicate. Hyaluronidase activity in human foreskin primary keratinocyte cultures was also quantitated. A 25-fold increase in hyaluronidase activity was observed in keratinocyte cultures induced to differentiate in high calcium (1.5 mM), compared to levels in low calcium (0.05 mM) media. The microtiter-based assay may be used as a routine clinical laboratory procedure.
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PMID:A microtiter-based assay for hyaluronidase activity not requiring specialized reagents. 929 25

We recently cloned the major hyaluronidase of human plasma, which we termed HYAL1. All hyaluronidase activity could be purified from human urine on an anti-HYAL1 monoclonal antibody column. However, urine contains two hyaluronidases of 57 kDa and 45 kDa, whereas plasma only contains the 57 kDa activity. Microsequencing confirmed that both urinary isozymes have N-termini identical to plasma hyaluronidase, but a second N-terminus was found in the smaller isozyme, apparently derived from the terminal 25 amino acids of HYAL1, at the C-terminus. The two polypeptides of the 45 kDa isozyme resulting from endoproteolytic cleavage of the 57 kDa isoform are presumably linked by disulfide bonds. Sperm contains two isozymes of the testicular hyaluronidase, PH-20, and the lower molecular weight isozyme is believed to be an endoproteolytically processed form of the larger protein. Analogously to PH-20, the smaller isozyme of HYAL1 is likely to be a proteolytically processed product of the larger isozyme.
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PMID:Purification and microsequencing of hyaluronidase isozymes from human urine. 940 39

Hyaluronidase activity has been detected for the first time in normal human dermal fibroblasts (HS27), as well as in fetal fibroblasts (FF24) and fibrosarcoma cells (HT1080). Enzymatic activity was secreted predominantly into the culture media, with minor amounts of activity associated with the cell layer. In both classes of fibroblasts, hyaluronidase expression was confluence-dependent, with highest levels of activity occurring in quiescent, post-confluent cells. However, in the fibrosarcoma cell cultures, expression was independent of cell density. The enzyme had a pH optimum of 3.7 and on hyaluronan substrate gel zymography, activity occurred as a single band corresponding to an approximate molecular size of 57 kDa. The enzyme could be immunoprecipitated in its entirety using monoclonal antibodies raised against Hyal-1, human plasma hyaluronidase. PCR confirmed that fibroblast hyaluronidase was identical to Hyal-1. The conclusion by previous investigators using earlier technologies that fibroblasts do not contain hyaluronidase activity should be reevaluated.
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PMID:Hyaluronidase expression in human skin fibroblasts. 1058 Dec 1

Hyaluronidase and hyaluronic acid, two substances thought to be strongly implicated in carcinogenesis, were assessed in the plasma of 35 patients with newly documented monoclonal gammapathy and in 25 control patients. A significant increase was found in plasma hyaluronidase activity in the patients with monoclonal gammapathy. A statistically significant positive correlation was found between hyaluronidase activity and monoclonal immunoglobulin levels in plasma. An increase in serum hyaluronidase activities may be a response to the deleterious effect of hyaluronic acid in cell migration and tumor progression. Further studies are needed to assess the value of hyaluronidase activity as a marker of tumor progression.
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PMID:Hyaluronidase activity in serum of patients with monoclonal gammapathy. 1102 Apr 70


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