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:3.5.1.4 (deaminase)
5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An enzyme preparation with affinity to a lysine column was detected from a DEAE-cellulose-adsorbed preparation of human seminal plasma containing plasminogen and plasmin. Two kinds of trypsin-like acidic arginine amidase activity with different affinity to lima bean trypsin inhibitor (LBTI) and aprotinin affinity column were detected from the DEAE-cellulose-adsorbed preparation after treatment of the lysine column. Two kinds of trypsin-like basic arginine amidase activity were also separated by the above-mentioned affinity adsorptions from a CM-cellulose-adsorbed preparation of human seminal plasma. The effect of calcium chloride on these two enzymes was different from human acrosin.
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PMID:Trypsin-like arginine amidases including plasminogen and plasmin in human seminal plasma by affinity adsorption and elution. 153 Mar 64

Basic arginine esterase (amidase) with a specific activity of 3.2 mumol N-alpha-tosyl-L-arginine methyl ester (Tos-Arg-Me) esterolysis per A280 was purified about 230-fold from a CM-cellulose absorbed preparation of human seminal plasma. The purified enzyme was a single band with an apparent molecular weight of 3.4-4.1 x 10(4). The amidolytic activity of this enzyme was suppressed by aprotinin, soybean trypsin inhibitor (SBTI), leupeptin, and antipain, while alpha 1-antitrypsin, ovomucoid trypsin inhibitor (OTI), EDTA, and chymostatin had no or weak effect. This enzyme hydrolyzed synthetic basic amino acid derivatives and N-alpha-tosyl-glycyl-L-prolyl-arginine-p-nitroanilide (Tos-Gly-Pro-Arg-pNA) and N-alpha-tert-butyloxycarbonyl-L-leucyl-L-prolyl-L-arginine-p-nitroanilid e (Boc-Leu-Pro-Arg-pNA) were the best substrates. The enzymatic characteristics of present enzyme were clearly different from tissue kallikrein, acrosin, and seminin in human semen.
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PMID:Basic arginine esterase from human seminal plasma: purification and some properties. 175 84

The objective of the present research was to identify a procedure whereby chicken acrosin could be purified. Acrosin, as evidenced by amidase activity, was extracted with urea most efficiently at a concentration of 6 M. Extraction efficiency was enhanced by spermatozoal lysis prior to admixture with 6 M urea. Lysis was induced by passage of spermatozoal suspensions through a French pressure cell. Acrosin was purified by using gel filtration, chromatofocusing, and affinity chromatography. Based on amidase activity, a 19-fold purification was obtained with a 28% recovery. Native electrophoresis resolved two major protein bands with proteolytic activity. The methods described afford the procurement of milligram amounts of chicken acrosin.
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PMID:Chicken acrosin: extraction and purification. 236 71

Zonae pellucidae isolated from porcine oocytes were solubilized in 0.15 M NaCl at pH 2.5. The zonal extract contained a protein with relatively low molecular weight, which inhibited the amidase activity of boar acrosin and bovine trypsin. This protein was immunologically related to the BUSI II proteinase inhibitor isolated from bull seminal plasma.
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PMID:Acrosin inhibitor in extract of the zonae pellucidae of porcine oocytes. 256 21

Acrosin, a sperm-specific acrosomal proteinase, has an essential role in the fertilization process. Low levels of acrosin appear to be associated with subfertility and infertility, and the acrosin activity of spermatozoa may potentially be a useful indicator of semen quality. The standard acrosin tests employed by research laboratories are too complicated and/or time consuming for clinical use; therefore, a simple assay has been developed to assess total acrosin activity (acrosin and activatable proacrosin). To perform the test, liquefied semen is centrifuged over Ficoll, the washed sperm pellet is suspended in a detergent (Triton X-100)-substrate (N-alpha-benzoyl-DL-arginine p-nitroanilide) buffer, pH. 8.0, and the amidase activity is determined spectrophotometrically after a 3-hour incubation period. Amidase activity can be inhibited with benzamidine, indicating that the activity is primarily or entirely due to acrosin. The absence of detergent in the incubation medium results in greatly reduced activity. The assay is repeatable, linear with increasing sperm concentration, sensitive to a lower limit of 2 x 10(6) spermatozoa, and the results correspond to those obtained with a standard acrosin extraction and assay technique. Storage of ejaculates at 3 to 6 C or at 22 to 24 C for 24 hours does not affect the acrosin activity significantly but much higher temperatures can cause a loss of activity. Freezing ejaculates results in a large decrease in sperm acrosin activity. Leukocytes show minimal activity in the assay. Sperm populations prepared by a swim-up procedure average approximately a 2-fold higher acrosin activity than the original ejaculates. Preliminary experiments indicate that the average sperm acrosin activity of ejaculates whose spermatozoa successfully fertilize human eggs in vitro is significantly higher than those that do not fertilize eggs.
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PMID:A simple, clinical assay to evaluate the acrosin activity of human spermatozoa. 274 33

Pronase-resistant low molecular weight stimulators for the activation of proacrosin to acrosin were found in rhesus monkey oviduct fluid collected before, during and after ovulation, but the presence of high concentrations of acrosin inhibitors before and after ovulation partly masked the stimulation in unfractionated fluid. This low molecular weight fraction of oviduct fluid had no detectable esterase or amidase activity by itself, and the stimulating factors were sensitive to digestion by hyaluronidase and chondroitin ABC lyase and were presumed to be glycosaminoglycans. Heparin and hyaluronic acid had similar effects. The presence of soluble glycosaminoglycans at the site of fertilization suggests that they may have a role in capacitation and fertilization.
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PMID:Stimulation of rhesus monkey (Macaca mulatta) proacrosin activation by oviduct fluid. 700 Oct 8

Analytical disk gel electrophoresis with staining techniques for amidohydrolase activity at pH 7.6 demonstrated that partially purified acrosomal extracts of ejaculated bull, boar, and human spermatozoa contained three, apparently four, and two fractions, respectively, with acrosin-like activity. Acrosin amidohydrolase activity is present in the gels incubated in the staining medium at pH 5.0. Some methods for the extraction of human acrosin have been compared. These consist essentially of the extraction by detergent treatment and the extraction by acid procedures. Acid extraction of human spermatozoa yields a higher amount of acrosin than does detergent extraction; the acrosin specific activity, extracted by these methods, seems to be similar.
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PMID:Multiple forms of boar, bull, and human acrosin. 700 80

Boar acrosin, a glycoprotein present in the acrosome of spermatozoa, tends to aggregate in the absence of detergents and lipids. Self-association products were analyzed electrophoretically by the method of Ferguson. Molecular weights ranging from 44 000 up to 237 000 were found, corresponding to acrosin monomer up to hexamer. Involvement of the active site of the serine proteinase in the formation of oligomers was demonstrated by active enzyme staining and determination of amidase activity of aggregated acrosin. Only monomeric acrosin proved to have full activity, while a marked decrease in specific activity was found upon aggregation. Hence, evidence is presented that acrosin has hydrophobic binding sites modulating the proteinase activity.
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PMID:Oligomerisation of boar acrosin. 700 57

Protease and basic amidase activity was found in the seminal plasma of the domestic turkey. Amidase activity, measured through use of N-alpha-benzoyl-DL-arginine-p-nitroanilide-HCL (BAPNA), was 23-28 times greater for turkey than for guinea fowl or chicken. Within the reproductive tract, seminal plasma from the vas deferens had much greater activity than testicular or epididymal fluids. Turkey seminal plasma enzyme (TSPE) purified by chromatography or isoelectric focusing showed three protein bands by PAGE, each resolving on SDS-PAGE into two subunits with molecular weights of approximately 28,000-32,000 and 38,000-44,000. One of the three proteins also contained a larger subunit (M(r) 76,000-81,000) thought to be transferrin. Turkey acrosin consisted of three subunits with molecular weights below 20,500. Acrosin, but not TSPE, was visualized in native gels with N-alpha-benzoyl-DL-arginine-beta-naphthylamide (BANA)/Fast Garnet stain. Michaelis constants (BAPNA) for TSPE, acrosin, and trypsin were 2.41 +/- 0.12 x 10(-4) M (n = 5), 4.96-6.03 x 10(-4) M (n = 2), and 6.76 +/- 0.95 x 10(-4) M (n = 6), respectively. TSPE, like acrosin and trypsin, was inhibited by benzamidine but not iodoacetamide. While all natural trypsin inhibitors tested inhibited acrosin, TSPE was not inhibited by ovomucoid from chicken or turkey egg white.
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PMID:Proteolytic enzymes in seminal plasma of domestic turkey (Meleagris gallopavo). 767 33

A mouse monoclonal antibody against boar acrosin and antiserum prepared to highly purified acrosin in female rabbits were used to detect the antigen in various fluids and tissues of boars using an indirect immunofluorescence technique. A strong reaction was found in fluid and epithelial tissue of the seminal vesicles as well as in the germinal cells in the testis. No immunoreactivity was detected in tissues of the epididymides and other organs of the boar. The antigens present in seminal vesicle fluid of boars were partially purified by column chromatography. It was demonstrated that two antigens differing in molecular mass were present and both possessed protease and amidase activity. The higher molecular mass antigen eluted from a gel filtration column in a volume identical to that of proacrosin. The same result was obtained in polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS-PAGE). The low molecular mass antigen was eluted from Sephadex G-75 column together with natural protease inhibitors corresponding in molecular mass to less than 20 kDa. The mobility of the antigen in SDS-PAGE was greater than that of chymotrypsin. It is assumed that the protease from seminal vesicle epithelial resembled acrosin in structure and function. Acrosin may therefore not be specific for spermatozoa.
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PMID:Serine protease activity in boar seminal vesicles and its immunological similarity to sperm acrosin. 802 64


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