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1

Digitale Medien

Phosphatidylcholine and phosphatidylinositol-specific phospholipases C of bull and rabbit spermatozoa (1992)

Hinkovska-Galchev, Vania ; Srivastava, Prakash N.

New York, NY [u.a.] : Wiley-Blackwell

Molecular Reproduction and Development 33 (1992), S. 281-286

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ISSN: 1040-452X

Schlagwort(e): Sperm (bull, rabbit) ; Plasma membranes ; Acrosomal membranes ; Phosphatidylinositol specific phospholipase C ; Phosphatidyl choline specific phospholipase C ; Life and Medical Sciences ; Cell & Developmental Biology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Biologie

Notizen: Acrosomal reaction is an essential prerequisite to fertilization. The changes in lipid composition of sperm membranes cause fusion of the plasma and outer acrosomal membranes that results in the exocytosis of acrosomal contents. We report that both bull and rabbit spermatozoa contain a phosphatidylcholine-specific phospholipase C (PC-PLC) that hydrolyzes L-α-dipalmitoyl-(choline-methyl-14C-153.0 Ci/mmol and a phosphatidyl-inositol-specific phospholipase C (Pl-PLC)) that hydrolyzes L-α-(Myo)-lnositol-2-3H (N)-5.2 Ci mmol. Pl-PLC from bull sperm acrosome has been purified 568 × fold with a specific activity 6.25 ± 0.6 nmol/min/mg protein, km 0.004 mM, and Vmax 12 nmol/min/mg protein. Both enzymes had optimum at pH 7.5. The activity of PC-PLC remained unaffected by varying concentrations of Ca2+, whereas Pl-PLC activity was significantly increased. The bulk of Pl-PLC was found to be associated with inner acrosomal membrane of bull and rabbit sperm, while PC-PLC was found in the outer acrosomal membranes in the bull sperm and the plasma membrane of the rabbit sperm. Both enzymes are compartmentalized in sperm cell. © 1992 Wiley-Liss, Inc.

Zusätzliches Material: 7 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/mrd.1080330308

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2

Digitale Medien

Phospholipids of rabbit and bull sperm membranes: Structural order parameter and steady-state fluorescence anistropy of membranes and membrane leaflets (1993)

Hinkovska-Galcheva, Vania ; Srivastava, Prakash N.

New York, NY [u.a.] : Wiley-Blackwell

Molecular Reproduction and Development 35 (1993), S. 209-217

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ISSN: 1040-452X

Schlagwort(e): Sperm (bull, rabbit) ; Plasma membranes ; Acrosomal membranes ; Phospholipids ; Membrane fluidity ; Life and Medical Sciences ; Cell & Developmental Biology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Biologie

Notizen: The plasma (PM), outer acrosomal (OAM), and inner acrosomal membranes (IAM) were isolated from rabbit and bull spermatozoa and the major phospholipids characterized. Choline-containing phospholipids, phosphatidylcholine (PC) and sphingomyelin (SM), constituted more than 60% of the total phospholipids (TPL) in all membranes of both species. Approximately more than 50% of PC in membrane preparations contained some form of ether linkage. Compared to OAM and IAM, cholesterol to phospholipid molar ratio was highest in PM of both species. Contrarily, protein to phospholipid ratio for PM was lowest compared to other membranes. The sphingomyelin to phosphatidylcholine ratio increased in the direction from PM to OAM to IAM. The hydrophobic fluorescent probe 1,6-diphenyl-1,3,5-hexatriene (DPH) was used to examine both the steady-state fluorescence anisotropy parameters and structural order parameter SDPH. The data showed higher rigidity in rabbit spermatozoa compared to bull spermatozoa (SDPH = 0.7582 and SDPH = 0.7326). In both species OAM had higher rigidity compared to the other two membranes (SDPH(OAM) = 0.7809, SDPH(PM) = 0.7308, and SDPH(IAM) = 0.7481 for bull; SDPH(OAM) = 0.8091, SDPH(PM)= 0.7857, and SDPH(IAM) = 0.7663 for rabbit). The inner leaflets of bull and rabbit spermatozoal membranes had significantly higher rigidity than the outer leaflets (for inner leaflet: rabbit-SDPH(PM) = 0.8391, SDPH(OAM) = 0.8149, and SDPH(IAM) = 0.7675; bull-SDPH(PM) = 0.8000, SDPH(OAM) = 0.7990, and SDPH(IAM) = 0.7990, and for outer leaflet: rabbit-SDPH(PM) = 0.7021, SDPH(OAM) = 0.7145, and SDPH(IAM) = 0.6867; bull-SDPH(PM) = 0.6986, SDPH(OAM) = 0.5980, and SDPH(IAM) = 0.7388). © 1993 Wiley-Liss, Inc.

Zusätzliches Material: 7 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/mrd.1080350215

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3

Digitale Medien

Purification and characterization of β-glucuronidase from bull seminal plasma and its role in fertilization (1994)

Rethinaswamy, Asokan ; Yang, Chul-Hak ; Srivastava, Prakash N.

New York, NY [u.a.] : Wiley-Blackwell

Molecular Reproduction and Development 38 (1994), S. 404-409

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ISSN: 1040-452X

Schlagwort(e): β-glucuronidase ; Seminal plasma ; Ovum ; Cumulus ; Fertilization ; Life and Medical Sciences ; Cell & Developmental Biology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Biologie

Notizen: Bull seminal plasma contains high levels of β-glucuronidase. The present study describes the isolation and characterization of β-glucuronidase, and its role in fertilization. β-glucuronidase was purified by ion exchange chromatography, saccharolactone-agarose affinity chromatography, and gel filtration. The specific activity of the purified enzyme was 4,414 μmoles/mg protein/min. The purified enzyme showed a single band on 7.5% PAGE. On SDS-PAGE, the enzyme appeared to consist of four identical subunits of Mr 75,000 each. The apparent Km and Vmax for β-glucuronidase were 0.4 mM and 5.7 μmol/min using phenolpthalein mono-β-glucuronic acid as the substrate. β-glucuronidase appeared to accelerate the cumulus dispersion in vitro. © 1994 Wiley-Liss, Inc.

Zusätzliches Material: 8 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/mrd.1080380408

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4

Digitale Medien

Partial purification and characterization of an alkaline proteinase from the rabbit testis (1985)

Ninjoor, Vyas ; Srivastava, Prakash N.

New York, NY : Wiley-Blackwell

Gamete Research 11 (1985), S. 69-82

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ISSN: 0148-7280

Schlagwort(e): Acrosin ; inhibitors ; alkaline ; proteinase ; acrosomal ; azocoll ; Life and Medical Sciences ; Cell & Developmental Biology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Biologie

Notizen: A proteolytic enzyme capable of cleaving intact proteins and synthetic substrates α-N-benzoyl-DL-arginine β-naphthylamide (Bz-Arg-NNap), α-N-benzoyl-L-arginine p-nitroanilde (Bz-Arg-NPhNO2), and α-N-benzoyl-L-arginine ethyl ester (Bz-Arg-OEt) was purified 92- fold from the rabbit testes. The enzyme exhibited optimal activity at pH 9.0 and 50°C. The polyacrylamide gel electrophoresis and sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the purified enzyme demonstrated multiple forms; the major band in the SDS-polyacrylamide gel electrophoresis corresponded to a Mt 48,000. The same value was established by the gel filtration over Sephadex G-75. The rabbit testicular alkaline proteinase (TAP) resembled acrosin in the hydrolysis of Bz-Arg-OEt. However, CaCl2, a potential stimulator of acrosin activity, inhibited the alkaline proteinase. The strong inhibitors of acrosin, eg pheny methyl sulphonyl fluoride (PMSF), tosyl lysine chloromethyl ketone (TLCK), and benzamidine did not inhibit the alkaline proteinase. TAP was activated by an acrosin inhibitor isolated from the rabbit testes. Since 0.5 M KCl was necessary for complete extraction of the enzyme and the bulk of the activity was present in 9,000g pellet of the testicular homogenate. The alkaline proteinase appeared to be associated with the membranous structures.

Zusätzliches Material: 4 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/mrd.1120110108

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5

Digitale Medien

Lysosomal hydrolases in reproductive organs during estrous cycle of the hamster (1984)

Rahi, Hamid ; Srivastava, Prakash N.

New York, NY : Wiley-Blackwell

Gamete Research 10 (1984), S. 57-66

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ISSN: 0148-7280

Schlagwort(e): Lysosomal hydrolases ; uterus ; ovary ; oviduct hamster ; Life and Medical Sciences ; Cell & Developmental Biology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Biologie

Notizen: Changes in the total protein content and the activities of lysosomal hydrolases (arylsulfatase, acid phosphatases, β-glucuronidase, β-N-acetylhexosaminidase, α-L-fucosidase, and β-galactosidase) of the hamster genital tract during the 4 days of estrous cycle and in hormonally superovulated hamsters were measured. Levels of lysosomal hydrolases in uteri and uterine fluid changed significantly during the cycle. Similar changes were observed in uterine wet weight and uterine proteins. The pattern of enzyme activities in both the ovary and the oviduct were different from those in uteri. In the ovary, most enzyme activities and the total protein concentration remained elevated after ovulation. Protein concentration and enzyme activities were significantly higher in the ovary, oviduct, and uteri of superovulated hamsters as compared to controls.

Zusätzliches Material: 4 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/mrd.1120100107

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6

Digitale Medien

Enhancement of the acrosome reaction of hamster spermatozoa by the proteolytic enzymes, kallikrein, trypsin, and chymotrypsin (1985)

Shinohara, Harumichi ; Yanagimachi, Ryuzo ; Srivastava, Prakash N.

New York, NY : Wiley-Blackwell

Gamete Research 11 (1985), S. 19-28

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ISSN: 0148-7280

Schlagwort(e): spermatozoa ; acrosome reaction ; proteolytic enzyme ; hamster ; Life and Medical Sciences ; Cell & Developmental Biology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Biologie

Notizen: The involvement of a kallikrein-kinin system in the motility of mammalian spermatozoa has been suggested by several investigators. We found that incorporation of kallikrein (0.1-1.0) unit/ml) in the sperm incubation medium did not enhance the motility of hamster spermatozoa that were already active. However, this enzyme significantly increased the incidence of the acrosome reaction. Trypsin (1.8-18 units/ml) and chymotrypsin (0.34-3.4 units/ml) also increased the incidence of the acrosome reaction, and accelerated its onset. Kinins (bradykinin and kallidin) added to the medium in a wide concentration range (1 ng/ml to 1 mg/ml) had no marked effects on either the motility or the acrosome reaction. A kallikrein-kinin system is apparently not of primary importance at least for the acrosome reaction. The enhancement of the acrosome reaction by exogenous proteinases may be due in part to accelerated removal or alteration of the sperm surface coat (glycoprotein) by the enzyme peior to the acrosome reaction. Exogenous proteinases may also act synergistically with endogenous (acrosomal) proteinases (and other enzymes) in altering membrane proteins and dispersing the acrosome matrix during the course of teh acrosome reaction.

Zusätzliches Material: 2 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/mrd.1120110103

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7

Digitale Medien

A modified column for sperm isoelectric focusing (1983)

Rahi, Hamid ; Srivastava, Prakash N.

New York, NY : Wiley-Blackwell

Gamete Research 7 (1983), S. 325-329

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ISSN: 0148-7280

Schlagwort(e): isoelectric focusing apparatus ; sperm ; protein ; density gradient ; Life and Medical Sciences ; Cell & Developmental Biology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Biologie

Notizen: A modified U-shaped column is described for efficient isoelectric focusing of spermatozoa, other cells, and protein. The washed spermatozoa of the rabbit showed a PI of 4.4. After sonication, heads and tails focused at same pH, indicating similar and equal charge.

Zusätzliches Material: 6 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/mrd.1120070404

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8

Digitale Medien

Isolation of the inner acrosomal-nuclear membrane complex from rabbit spermatozoa (1983)

Rahi, Hamid ; Sheikhnejade, Gholamreza ; Srivastava, Prakash N.

New York, NY : Wiley-Blackwell

Gamete Research 7 (1983), S. 215-226

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ISSN: 0148-7280

Schlagwort(e): sperm ; cytoplasmic droplet ; membrane ; acrosome ; nucleus ; decondensation ; rabbit ; Bio-Glas 2500 ; Life and Medical Sciences ; Cell & Developmental Biology

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Biologie

Notizen: Rabbit spermatozoa were passed through a Bio-Glas 2500 (BG) column to yield pure cytoplasmic droplets and consequently the droplet-free spermatozoa. Rapid decondensation of sperm nuclei was achieved by 1 mM dithiothreitol (DTT) and 1.5 M NaCl. This treatment caused removal of the plasma and the outer acrosomal membranes. The viscosity of decondensed nuclei was reduced by pancreatic DNase. Further elution of the suspension from BG column yielded a membrane complex. On the basis of electron microscopic observations and the enzyme analysis, these membranes appeared to be the inner acrosomal-nuclear membrane complex (IANC). The IANC was also prepared from isolated sperm head by DTT-NaCl and Dnasetreatment and low-speed centrifugation.

Zusätzliches Material: 9 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/mrd.1120070303

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