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)

Microbial hyaluronidase (EC 4.2.2.1) was isolated from the culture fluid of Staphylococcus aureus 0-15 with purification by precipitation with 1 volume of ethyl alcohol, chromatography on DEAE cellulose and ultrafiltration through DA type membranes with the pore size of 0.65 micron ("Millipore") and PM-10 membranes ("Amicon"). The specific activity of the enzyme averaged to 2700 turbidimetric units or 32130 IU. 6585-fold purification of the enzyme was performed. The optimum action on hyaluronic acid was observed at pH 5.0-6.5. Hyaluronidase was inhibited by Fe3+, Fe2+ and Cu2+, activated by Ca2+ and stabilized by 0.15 M NaCl. It was detected that the enzyme had two molecular forms with the isoelectric points of 5.4 and 6.5 and the molecular weights of 55 000 and 24 0000 D respectively. The glycoprotein nature of the enzyme was shown. The immobilized form of hyaluronidase on activated polyglucin, a soluble biocompatible polymer was prepared. The form is characterized by higher thermostability.
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PMID:[Purification and properties of staphylococcal hyaluronidase]. 396 93

Hyaluronidase (hyaluronate 4-glycanohydrolase, EC 3.2.1.35) has been isolated from pig liver and purified 1720-fold with an overall yield of 9.5%. The enzyme was purified using an acid-extraction technique followed by successive chromatography on DEAE-cellulose, two boronate affinity columns and Sephadex G-75. This final preparation, which was essentially homogeneous as determined by gel electrophoresis, was a single subunit enzyme of apparent molecular weight 70 000 with an isoelectric point of 5.0. No contaminant enzymes capable of degrading glycosaminoglycans could be detected in the final preparation. The substrate specificity of the enzyme was the same as for bovine testicular hyaluronidase; however, both the Km and V values were significantly lower for the pig liver enzyme with all of the substrates tested (hyaluronate, chondroitin 4-sulphate, chondroitin 6-sulphate). A full kinetic analysis of the enzyme using hyaluronate as a substrate showed that the activity of pig liver hyaluronidase was uncompetitively activated by either protons or NaCl.
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PMID:The purification and some properties of pig liver hyaluronidase. 397 Sep 70

Cultured myoblasts were found to exhibit extensive, Streptomyces hyaluronidase-sensitive pericellular coats as revealed by exclusion of particles (fixed red blood cells). These coats are not discernible subsequent to fusion of the myoblasts to form myotubes. The myoblasts contained 2.5 times more hyaluronate attached to their cell surface than myotubes when the data was expressed per unit of protein, but no change in hyaluronate was evident on a per DNA basis. Hyaluronidase activities in the cultures were equivalent when expressed per unit of protein. We conclude that, although the myotubes accumulate larger amounts of protein than myoblasts, there is no compensatory increase in hyaluronate.
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PMID:Loss of hyaluronate-dependent coat during myoblast fusion. 397 68

Effects of hyaluronidase on myocardial water content and distribution, and on coronary vascular hemodynamics and endothelial cell transport function were assessed in isolated rabbit hearts during 3.5 hours of reperfusion after 30 minutes of global, no-flow ischemia. In nonischemic control hearts, perfusion pressure, left ventricular end-diastolic pressure, maximum +dP/dt, and intravascular clearance of radiolabeled albumin remained constant during 5 hours of continuous perfusion, while the mean-transit time and vascular into extravascular space clearance of radiolabeled albumin increased 1.5X and 2.5X baseline, respectively. During reperfusion after 30 minutes of no flow, perfusion pressure increased 53% and interstitial fluid volume increased 2-fold, while left ventricular end-diastolic pressure and maximum +dP/dt returned to control levels. The rate of intravascular clearance of radiolabeled albumin decreased 38%, and the mean-transit time and vascular-into-extravascular space clearance of albumin increased approximately 3X and 5X baseline, respectively. Hyaluronidase blocked the ischemia-reperfusion-induced increases in total water content and in interstitial fluid volume and reduced the increases in perfusion pressure and mean-transit time of radiolabeled albumin by 40% and 45%, respectively, but did not prevent the increase in albumin vascular-into-extravascular space clearance and the decrease in albumin clearance from the coronary vasculature. These findings indicate that hyaluronidase does not prevent ischemia-reperfusion-induced increases in albumin permeation of the coronary vasculature, and suggest that its protective effect on ischemic myocardium is mediated, instead, by reducing interstitial edema and vascular resistance.
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PMID:Hyaluronidase does not prevent deterioration of vascular functional integrity during reperfusion after no-flow ischemia in isolated rabbit hearts. 400 93

Hyaluronidase release was used as an index of acrosomal membrane damage during cold shock of epididymal boar sperm and ejaculated sperm from intact and vesiculectomized boars. Sperm were also incubated with seminal plasma from intact and vasectomized boars to examine the contributions of male accessory gland secretions. Acrosomal membranes of epididymal sperm were more resistant to cold shock than those of ejaculated sperm. Only 36% of the hyaluronidase released by ejaculated sperm was released by the epididymal sperm in spite of similar hyaluronidase content of the sperm. Preincubation of epididymal sperm in seminal plasma from both intact and vasectomized boars increased resistance to cold shock by 60 to 80%. Initial dilution of epididymal sperm with seminal plasma, rather than Ringer-fructose buffer, was associated with low progressive motility and with retention of cytoplasmic droplets. In contrast, acrosomal membranes of ejaculated sperm from intact and vesiculectomized boars exhibited similar sensitivity to cold shock, releasing hyaluronidase capable of forming .20 and .19 mumol N-acetylglucosamine from hyaluronic acid/10(8) sperm in 8 min. Moreover, seminal plasma from vasectomized boars had no effect on acrosomal sensitivity to cold shock of ejaculated sperm from vesiculectomized boars.
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PMID:Effect of male accessory gland secretions on sensitivity of porcine sperm acrosomes to cold shock, initiation of motility and loss of cytoplasmic droplets. 400 68

The treatment of compartment syndromes in which elevation of intracompartmental pressure occurs is by surgical fasciotomy. This is a relatively simple procedure but may be associated with complications. This study aimed at developing an alternative method to decompress a compartment by use of the enzyme hyaluronidase. Autologous plasma was infused into the anterolateral leg compartments of six dogs to simulate compartment syndromes of 80 mmHg. Pressure decay after pressurization was recorded. The compartment pressures were then again raised to 80 mmHg by subfascial injections of 1500 units hyaluronidase in 2 ml saline injected into one compartment and 2 ml saline only into the control side. Pressure decay was again recorded. On the experimental side, a significantly faster decay rate occurred after hyaluronidase injection than after initial pressurization; 8.0 +/- 1.3 (S.E.M.) versus 3.4 +/- 0.4 (S.E.M.) mmHg/min (p less than .01). Pressure decay after hyaluronidase injection was significantly faster than after the same volume injection on the control side, over both a four-minute period (8.0 +/- 1.3 [S.E.M.] versus 4.1 +/- 0.6 [S.E.M.] mmHg/min [p less than .03]) and a 25-minute period (2.1 +/- 0.3 [S.E.M.] versus 1.3 +/- 0.1 [S.E.M.] mmHg/min [p less than .03]). Hyaluronidase removes hyaluronic acid molecules from the leg compartment fascia and, by facilitating fluid flow from the compartment, causes decompression. Hyaluronidase may then have a place in the prophylaxis and treatment of compartment syndrome, thus avoiding anesthesia and surgery.
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PMID:Decompression of an experimental compartment syndrome in dogs with hyaluronidase. 401 43

The effects of UVA and chlorpromazine on the activity of hyaluronidase were investigated. Hyaluronidase was slightly activated by UVA alone. It was also activated by chlorpromazine, but the activation was enhanced by concomitant UVA irradiation. By pre-irradiation of chlorpromazine, it was found that a stable photoproduct of chlorpromazine was formed that activated hyaluronidase. As activation of hyaluronidase has been described in relation to tissue inflammation, the onset of chlorpromazine-induced photosensitivity may, in part, be related to the hyaluronidase activating effect of chlorpromazine plus UVA.
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PMID:Photoactivation of hyaluronidase by chlorpromazine. 402 15

The length-tension properties of alveolar wall from normal cats were studied before and after exposure to enzymes naturally found in mammals (elastase, trypsin, collagenase, hyaluronidase). Hyaluronidase effected little change while all the proteolytic enzymes altered the mechanical properties of lung tissue. Collagenase removed the "mechanical stop" and the alveolar walls fractured at low forces. The properties of wall exposed to trypsin resembled those of elastase-treated tissue. Elastase increased the extension necessary to reach a given force and increased the maximum length (L(max)) and resting length (L(o)). Maximum extensibility (lambda(max)), the ratio of L(max) to L(o), fell with both elastase and trypsin digestion. A reduction in lambda(max) simulates the changes in alveolar wall properties seen in the lungs of the aged and in those with an irreversible diffuse obstructive pulmonary syndrome (DOPS(I)). Unlike these states, however, the energy loss in stretching alveolar wall increased with elastolysis. Furthermore, the changes in L(o) necessary to effect a change in lambda(max) of alveolar wall comparable to that seen in DOPS(I) were excessive. The altered tissue properties that occur in man with obstructive pulmonary syndromes could not be produced with these proteolytic enzymes or with hyaluronidase.
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PMID:Simulation of tissue properties in irreversible diffuse obstructive pulmonary syndromes. Enzyme digestion. 435 77

1. Electrophoresis of chondroitin sulphate, before and after partial degradation with testicular hyaluronidase, revealed charge heterogeneity of the degraded but not of the intact polymer. 2. Hyaluronidase-treated chondroitin sulphate was fractionated by gel chromatography. Two subfractions which were essentially monodisperse with regard to molecular weight (values of 8600 and 4800, respectively) were separated further by chromatography on Dowex 1. The resulting subfractions differed considerably with respect to their sulphate/disaccharide molar ratios. 3. Amino acid and neutral-sugar analyses of the Dowex 1 subfractions showed that the less sulphated fragments contained the carbohydrate-protein linkage region, whereas the high-sulphated fragments essentially lacked this constituent. It was concluded that chondroitin sulphate contains relatively less sulphate in the vicinity of the carbohydrate-protein linkage region than in the more peripheral portion of the polysaccharide chain.
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PMID:The distribution of sulphate residues in the chondroitin sulphate chain. 516 40

Hyaluronidase activity was examined in 109 specimens of human semen of various sperm densities, seminal plasma, and spermatozoa sedimented by centrifugation. We used a modification of a method originally devised for estimation of hyaluronidase activity in Clostridia and which was bases on measurements of the area of hyaluronate digestion in agar plates. Enzyme activities in both semen and seminal plasma increased with increase in sperm density. The activity in seminal plasma, which appeared promptly after liquefaction and represented enzyme released from spermatozoa, ranged from 31% to 61% of the activity in semen. Activities of spermatozoa in sediments exhibited lower values than those calculated for sperm of whole semen, possibly due to leakage. Both activities, calculated per million sperm cells, gradually increased with decrease in sperm density. The possibility that with severe oligozoospermia the acrosome may become less prone to enzyme release or that the initial activity per cell may increase is discussed. These phenomena would represent additional characteristics of oligozoospermia.
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PMID:Estimation of hyaluronidase activity of human semen and its relationship with sperm density by means of a simplified method. 612 24


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