Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The study of bull semen revealed that the activity of alkaline phosphatase in the semen plasma and spermatozoa did not change, however, upon incubation at 39 degrees C for at least 5 hours the activity of the enzyme dropped nearly 10 times. The activity of GOT in both plasma and spermatozoa rose after deep freezing, but the difference recorded were statistically insignificant. Upon incubation of semen at 39 degrees C in the course of five hours the activity of this enzyme decreased, although insignificantly. The differences were likewise insignificant with the drop of GPT following deep freezing. It was concluded that the changes with all three enzymes cannot be used as reliable markers of the injury of spermatozoa following deep freezing.
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PMID:[Enzyme activity of the seminal fluid of bulls after deep freezing and incubation at 39 degrees C]. 381 Dec 7

A 15-kilodalton protein has been identified as a major component of the residual protein fraction of mouse epididymal/vas spermatozoal heads, demembraned by treatment with Triton X-100 and sequentially extracted with 1 M NaCl/2-mercaptoethanol/DNase I. Two-dimensional electrophoresis of that protein before and after treatment with alkaline phosphatase indicated that it is present in epididymal/vas spermatozoa as a series of five differentially phosphorylated molecules with pI 6.0-7.0. Cyto-immunofluorescence with an affinity-purified antibody to the 15-kDa protein localized that protein to a circumscribed region of the demembraned mouse sperm head mediad from the dorsal margin. By radioimmunoassay, the 15-kDa protein was shown to be sperm-unique and species-specific. The antibody was nonreactive with homogenates of meiotic spermatogenic cells and round spermatids (stages 1-11) but was reactive with a non-phosphorylated 15.5-kDa protein of elongating spermatids (stages 12-16) and testicular spermatozoa. Following alkaline phosphatase treatment, the spermatozoal 15-kDa protein migrated to the position of the spermatidal 15.5-kDa protein on a sodium dodecyl sulfate gel. Thus, we conclude that the 15-kDa protein of mouse spermatozoa is synthesized during the elongation phase of spermiogenesis (stages 12-16) and is phosphorylated in the terminal period of that phase and/or after excursion of spermatozoa from the seminiferous tubules.
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PMID:Proteins of demembraned mouse sperm heads. Characterization of a major sperm-unique component. 388 61

A simple and reliable enzyme-linked immunosorbent assay (ELISA) for the detection of antisperm antibodies has been developed in our laboratory. The antigen for the solid phase was produced by sperm sonication while antihuman globulin conjugated to alkaline phosphatase was used as the developing reagent. The conditions and reagents of the assay were chosen to give a mild treatment of the antigen, simple manipulation during washing steps, and nontoxic and readily available reagents. The results were compared to a conventional microscopical method routinely used in our laboratory that detects agglutinating antibodies to human spermatozoa. In 96% of all cases antibodies detected by the microscopical method were also detected by ELISA. Moreover there were some cases where no antisperm antibodies could be demonstrated by microscopy, but gave a positive reaction with ELISA. These were usually cases of unexplained oligospermia, agglutinates in the ejaculate, and bad motility or low viability of the sperms. These results, and also titration experiments of positive samples demonstrate the higher sensitivity of the ELISA by comparison with microscopical methods.
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PMID:An enzyme immunoassay for the detection of antisperm antibodies. 389 81

This study concerns the effect of graded doses of estrogen, alone or in combinations with progesterone, on the biochemical composition of the rat seminiferous tubules. Data on the accessory genital organs and pituitary gonadotrophic activity are added. Adult male albino rats received estradiol dipropionate (.1, 1 and 5 mcg/rat) injected intramuscularly, in .1 ml olive oil, daily for 30 days. Animals given the 5 mcg dose were given a 30 day rest period to determine reversibility of effects. In another group estrogen (5 mcg/rat) and progesterone (1 mg/rat) were given concurrently but at different sites for 30 days. Controls received vehicle only. Animals were sacrificed 24 hours after the last injection or rest period and genital organs and the pituitary were removed for study. A progessive reduction in testis weight with dosage was found after estrogen or the combination (p is less that .01). The low dose (.1mcg) had an inconsistent effect on spermatogenesis and endocrine function of the testis. Diameter of the tubules was reduced. Spermatogenesis was arrested in 25% of the tubules at the spermatid of secondary spermatocyte stage. Some normal spermatozoa were seen. Tunica propria was thickened. Some Leydig cells showed atrophy. Vascularity was increased. The median dose (1 mcg) caused spermatogenic arrest at the spermatid or secondary spermatocyte stage but the Sertoli cells were prominent. Only a few spermatozoa were seen. There was some desquamation of seminiferous epithilium. Tubular diameter was still further reduced and the tunica propria thickened. Leydig cells were atrophied. Few spermatozoa were found although 25-30% showed some spermatogenesis. The high dose (5 mcg) caused marked reduction in the diameter of the tubules. Spermatogenesis was arrested at the primary spermatocyte or spermatogonial stage. The tunica popria was much thickened. There was much desquamation and tubular lumeus were filled with debris. The Sertoli cells were hypertrophied. The Leydig cells were atrophied. The tunica albuginea was thickened. There were no spermatozoa. In the recovery group estrogen effects had disappeared, but the tubular diameter remained reduced. Tunica propria was normal. Spermatogenesis progressed to the spermatid stage and in 50% of the tubules many spermatozoa were present. The Leydig cells appeared normal. However spermatozoa were not found in the vas defereus. The histological appearance of the teatis in the estrogen and progesterone group was of the high dose estrogen type but with arrest of spermatogenesis at the spermatid, spermatocye or spermatogonial stage. The Sertoli cells remained hypertrophied. Leydig cells were atrophic. The large blood vessels were engorged. Weight of organs returned almost to normal. Estrogen .1 and 1 mcg had no effect on pituitary weight or gonadotrophin content. The high dose (5 mcg) alone or with progesterone caused a significant increase in pituitary weight (p is less than .0). Estrogen alone (5 mcg) caused a significant decline in pituitary gonadotrophin content (p is less than .0) but the combined therapy had no effect. None of the biochemical constituents of the seminiferous tubules showed any change after injection of .1 mcg of estrogen but 1 mcg dose caused an increase in protein nitrogen, alkaline phosphatase activity and total lipids. The high dose (5 mcg) provoked higher levels.
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PMID:Effect of estrogen on biochemical composition of the rat seminiferous tubules. 514 19

The antispermatogenic effects of 2, 4-dinitro-6-tert-. butylphenyl methanesulfonate (HE-166) were studied in Sprague-Dawley rats. They were fed 25, 100 and 400 ppm of HE-166 in the basal died for one year. Laboratory data showed no significant changes except for increases in gamma-globulin, alkaline phosphatase, GOT and GPT values in the 100 ppm group. Macroscopically, significant changes were found in the testes in the experimental group, which showed marked atrophy. Histologically, the testes were filled with fibrin exudate in the stroma and there was reduced spermatogonia, cellular debris and giant cells, and even calcification, depending on the dose of HE-166. The anti-fertility effects of HE-166 were also observed by mating rats and checking the pregnancy rate during three generations. These effects might be due to the direct cytotoxic effect of HE-166 on post-meiotic cells as epididymal spermatozoa and testicular sperm and spermatids. As far as tumor incidence was concerned, one case of fibroadenoma of the mammary gland, one case of leiomyosarcoma in the uterus in the 100 ppm group and one case of leiomyoma in the uterus in the 25 ppm group developed at around 8 months, but no other tumors developed.
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PMID:The antispermatogenic effect and toxicity of 2, 4-dinitro-6-tert-butylphenyl methanesulfonate on Sprague-Dawley rat. 609 Jun 86

The plasma membranes of ram spermatozoa were disrupted in a hypotonic EDTA medium and isolated by using a two-phase polymer system of dextran--polyethyleneglycol. The plasma membranes obtained were of a relatively high degree of purity (approximately 70%) as judged by electron microscopy observations and measurements of the marker enzymes alkaline phosphatase, ATPase and AMPase. The activity of succinate cytochrome C reductase, a marker of mitochondrial membranes, was very low.
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PMID:Isolation of plasma membranes from ram spermatozoa by a two-phase polymer system. 616 59

The screening of autopsy specimens, vaginal, buccal, and rectal swabs, for the presence of seminal fluid in rape homicide investigations utilizing classical techniques can lead to erroneous results. In the absence of spermatozoa, techniques are needed which can help to identify seminal fluid. This report illustrates the use of a multi-enzyme electrophoretic approach identifying seminal acid phosphatase (SAP) and lactic acid dehydrogenase (LDH-X) as an initial screening procedure. Subsequent analyses for the presence of acid and alkaline phosphatase (semiquantitative) yield information which can help identify false-positive SAP's. Additionally, salivary amylase can be tentatively identified using the same multi-enzyme procedure which informs the investigator of possible salivary contamination of the sample and possible erroneous PGM results. Statistics utilizing the multi-enzyme approach in case work are also presented.
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PMID:A multi-enzyme electrophoretic system for the identification of seminal fluid from postmortem specimens. 617 21

ATPase of 14S dynein, extracted from spermatozoa of the sea urchin, Hemicentrotus pulcherrimus, and partially purified by sucrose density gradient centrifugation, was inhibited non-competitively by palmitoyl CoA at concentrations higher than 20 microns, and was stimulated at concentrations between 2 microns and 10 microns. The effects of palmitoyl CoA on dynein ATPase were reversed by bovine serum albumin (1 mg/ml) and spermine (0.1 and 1 mM). Myristoyl CoA exerted effects similar to those of palmitoyl CoA. Short chain fatty acyl CoAs, such as butyryl CoA, propionyl CoA and acetyl CoA, CoA, Na-palmitate, Na-myristate, and palmitoyl carnitine had hardly any effect on dynein ATPase. Palmitoyl CoA failed to inhibit purified CF1 ATPase from chloroplasts of spinach, ATPase of rat liver mitochondria and alkaline phosphatase from calf intestine.
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PMID:Inhibition by palmitoyl CoA of dynein ATPase from sea urchin spermatozoa. 621

Daily oral administration of 1 mg/kg b.w. of cyproterone acetate and simultaneously administered testosterone enanthate (2 mg/kg b.w./15 days; i.m.) to adult male langur monkeys over a period of 90 days caused a gradual decrease in the count (to azoospermia) and motility of spermatozoa, concurrently with an increase in the percentage of non-motile as well as abnormal and immature sperm. Semen weight, volume, seminal fluid volume and circulating testosterone levels decreased nonsignificantly. Semen pH, libido and body weight remained unimpaired. The levels of SGOT, SGPT, serum alkaline phosphatase, LDH, bilirubin, Na+, K+ and hematological values did not alter significantly. All the changes were reversible. The results indicate that the combination regimen seems to affect the fertility in two ways, i.e. by inhibiting spermatogenesis in the testis and maturation process in the epididymis without altering the androgenicity.
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PMID:Effects of cyproterone acetate with combination of testosterone enanthate on seminal characteristics, androgenicity and clinical chemistry in langur monkey. 623 11

Antiserum was raised in rabbits against an egg-yolk lipoprotein fraction previously shown to have cryoprotective properties. It was used in conjunction with alkaline phosphatase-conjugated goat anti-rabbit IgG to demonstrate lipoprotein interaction with bovine spermatozoa. The lipoprotein bound firmly to spermatozoa and was not removed by extensive washing, suggesting that the lipoprotein had become irreversibly associated with the sperm membranes.
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PMID:Immunochemical investigation of the interaction of egg-yolk lipoproteins with bovine spermatozoa. 636 22


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