Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Three different autoantigens (S, P and T), extracted and separated from guinea-pig spermatozoa, give rise to an autoimmune aspermogenic orchitis (AIAO) when injected with Freund's complete adjuvant (FCA). They also induce specific antibodies, such as anaphylactic (with S and P), complement-fixing (with P and T), spermotoxic (only with T) and precipitating and Arthus-inducing antibodies (only with P). Passive transfer of AIAO was attempted by injections of high total doses (15-20 ml per animal) of immune sera directed against one of the three antigens. Successful passive transfers were evaluated by the intensity of the epididymal and testicular lesions which were comparable to the actively induced ones, and by the rapid appearance of these lesions in less than 1 week and their lasting for at least 2 weeks. The disease was passively transferred with anti-P immune sera in as many as 64% of these cases and up to 40% with anti-T immune sera. Anti-S sera did not transfer AIAO more than did control normal and anti-DNP-BGG guinea-pig sera. The incidence and intensity of lesions were greatly for anti-P or slightly for anti-T increased by pretreating the future recipients with FCA. Hyperimmune sera are considerably more effective than early sera even when the latter are used in a time sequence reproducing that of the active reaction. The orchitogenic acitvity of anti-T sera appears to be localized in IgG2 DEAE fractions while that of anti-P has been found only in Ig1-containing DEAE fractions.
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PMID:Passive transfer of autoimmune aspermogenic orchiepididymitis (AIAO) by antispermatozoa sera. Influence of the type of autoantigen and of the class of antibody. 13 89

There appear to be two classes of protein kinases in rat heart and adipose tissue, types I and II. Type I elutes from DEAE-cellulose at smaller than 0.1 M NaCl and type II at greater than 0.1 M NaCl. The type I enzyme is more readily dissociated by salt or histone than is the type II enzyme. If the type I kinase is first dissociated by cAMP, the subunits reassociate very slowly at 0 degrees C on removal of the cAMP by Sephadex G-25 chromatography, whereas those of type II reassociate very rapidly. Rat heart contains mostly type I and a small amount of type II enzyme, whereas adipose tissue contains almost exclusively the type II enzyme. The adipose tissue enzyme resembles the heart type II kinase in all of the above properties, although the two enzymes are not identical as indicated by slight differences in elution patterns from DEAE-cellulose columns. Incubation of rat epididymal adipose tissue with low concentrations of epinephrine (0.11 muM) increases glycerol production and the fraction of the protein kinase in the active form (activity ratio). The change in cAMP under these conditions is not statistically significant. The presence of insulin inhibits the epinephrine effect on glycerol production and protein kinase but has no measurable effect on cAMP levels. Incubation of adipose tissue with high epinephrine concentrations (11 muM) increases the cAMP level, the protein kinase activity ratio, and glycerol production. Under these conditions insulin decreases the cAMP level and kinase activity ratio but does not reduce glycerol production. The data suggest that very small changes in the tissue cAMP level, undetectable by the assay method, are magnified during the stepwise activation of glycerol output aided possibly by cooperative effects between cAMP and protein kinase. The procedure developed for determining the state of activation of the cAMP-dependent protein kinase in adipose tissue must be modified by reducing the salt concentration of the buffers in order to carry out similar studies in the heart. This reflects the different types of protein kinase in the two tissues. The addition of charcoal to crude extracts of heart prevents protein kinase activation by added cyclic AMP. Charcoal should therefore prevent any activation that could occur if any sequestered cAMP were released during homogenization. Charcoal addition thereby provides a means to distinguish intracellular cAMP activation of the kinase from that which might occur following cell rupture. If epinephrine-perfused hearts are homogenized in the presence of charcoal, epinephrine stimulation of the protein kinase is only slightly decreased. This indicates that the protein kinase is activated intracellularly by cAMP and suggests that all of the cAMP in the cell is available to the protein kinase; i.e., cAMP is not released during homogenization.
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PMID:Hormonal regulation of adenosine 3',5'-monophosphate-dependent protein kinase. 16 70

Testicular androgen-binding proteins (ABP) in rabbit testis, caput epididymis and efferent duct fluid (EDF) were compared to a similar androgen-binding protein TeBg) in rabbit serum. The affinity of these proteins for 5alpha-dihydrotesterone (DHT) at 0 degrees C (KaABP = 1.6 X 10(9) M-1 and KaTeBG = 1.9 X 10(9) M-1) and their steroid specificities were similar (DHT greater than androstanediol greater than progesterone and androstenedione). ABP and TeBG had also almost identical Stokes radii (42.8 +/- 1.2 and 43.9 +- 0.8 A, respectively), sedimentation coefficients (4.7 +/- 0.2 S and 4.4 +/- 0.2 S, respectively) and electrophoretic mobility (Rf = 0.4 in 6 1/2% polyacrylamide gels). Calculation of molecular weights from Stokes radii and sedimentation rates indicated a molecular weight of 74,000 (69,000-78,000) for TeBG and 76,000 (71,000-82,000) for ABP. The corresponding frictional ratios were 1.61 for TeBG and 1.55 for ABP assuming a partial specific volume (v) of 0.70 cm3/g. Polyacrylamide gel electrophoresis (PAGE) at different gel concentrations gave a mean molecular radius of 2.74 nm, also indicating a molecular weight of about 75,000 (v = 0.70 cm3/g. ABP and TeBG could not be separated by PAGE; however, partial separation of ABP and TeBG was achieved by isoelectric focusing and ion-exchange chromatography on DEAE-cellulose. TeBG focused at pH 5.4, whereas ABP formed a distinct peak of bound radioactivity at pH 4.7. Also by ionexchange chromatography, ABP in both testis and epididymal supernatants was shown to have an apparently higher surface charge than TeBG in rabbit serum. The concentration of ABP in efferent duct fluid (2 X 10(-7) M = 60 pmol/mg protien) was much higher than TeBG in male rabbit serum (5.2 X 10(-8) M = 0.7 pmol/mg protein). These findings ruled against the possibility that ABP in the testis and epididymis could have been derived directly from serum. It is concluded that ABP and TeBG are very similar if not identical proteins both serving as transport and carrier proteins in their respective compartments.
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PMID:Testicular androgen-binding protein (ABP): comparison of ABP in rabbit testis and epididymis with a similar androgen-binding protein (TeBG) in rabbit serum. 16 2

Insulin was modified with d-biotin-N-hydroxysuccinimide ester in dimethylformamide. Mono-, di-, and triacylated insulins were separated by preparative isoelectric focusing. Monoacylated derivatives (isoelectric point 5.1) were fractionated twice on DEAE-cellulose to yield pure N epsilonB29-biotinylinsulin. The structure of the product was established by amino acid analysis before and after deamination. N epsilonB29-biotinylinsulin had biological activity indistinguishable from insulin on glucose oxidation and lipid synthesis assays using isolated rat epididymal fat cells. Complexes of N epsilonB29-biotinylinsulin with avidin, having essentially all but one binding site filled with biotin, were prepared in order to obtain a 1:1 insulin:avidin ration. The elicited identical maximal biological responses, but showed a potency decreased to 5% of that of insulin. Such complexes conjugated with ferritin will provide a useful tool in the development of electron microscopic stains of insulin receptors.
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PMID:N epsilonB29-(+)-biotinylinsulin and its complexes with avidin. Synthesis and biological activity. 62 Nov 98

Three separate acid phosphatases were found in the rat epididymal homogenate after fractionation by DEAE- and CM-cellulose chromatography as well as by electrophoresis. They differed from each other also in substrate specificity. This can possibly be utilized as an aid in their differential quantitation. Some other species including man, dog, rabbit, guinea pig and mouse also had a multiple composition of epididymal acid phosphatases.
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PMID:Acid phosphatases of the rat epididymis. I. Fractionation and substrate specificity. 100 65

One of the ligand molecules was purified from mouse cauda epididymal sperm for an indication of its inhibitory activity in sperm-egg binding. It was isolated in an electrophoretically homogeneous form by ionophore A23187 treatment of sperm, sedimentation by ultracentrifugation, solubilization by 2% Nonidet P-40 (NP-40), repeated ion exchange chromatography on DEAE-Sepharose CL-6B and gel filtration on Sephacryl S-200. The purified ligand exhibited a molecular mass of 60,000 dalton by gel filtration and 67,000 dalton by sodium dodecyl sulfate polyacrylamide-gel electrophoresis (SDS-PAGE). This molecule was radioiodinated by the lactoperoxidase method and assayed the binding ability to egg zona pellucida. The labeled ligand specifically bound to both cumulus-free egg zona pellucida and isolated-zona pellucida of unfertilized egg in a similar extent, but didn't bind to 2-cell egg zona pellucida. The maximal binding site of ligand per egg zona pellucida was estimated about 660000 molecules by Scatchard plot analysis.
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PMID:Studies on mouse sperm binding molecule (ligand) to egg zona pellucida. II. Purification of ligand molecule from cauda epididymal sperm. 183 61

A previous study has characterized the major 47 kDa anti-sticking factor (ASF-I) from goat cauda-epididymal plasma (Roy, N., and Majumder, G.C., Biochim. Biophys. Acta, 991:114-122, 1989). This study reports the purification and characterization of ASF-II, another anti-sticking factor from the goat epididymal plasma. ASF-II was purified to apparent homogeneity by using concanavalin A-agarose affinity chromatography, DEAE-cellulose chromatography, alumina gel adsorption, and isoelectric focussing techniques. It showed a single protein band by both non-denaturing and SDS-polyacrylamide gel electrophoresis. ASF-II showed a molecular weight of 36,000 and a sedimentation constant of 2.4S. ASF-II is largely stable to heat treatment and it is a specific glycoprotein having high affinity and specificity for its anti-sticking action. At saturating concentration (1 nM) it inhibited adhesion of nearly 50% of spermatozoa to the glass surface of the haemocytometer counting chamber. Both the protein and sugar parts of the factor are essential for the anti-sticking activity since it lost its activity completely when treated with trypsin, L-fucosidase, or mannosidase. ASF-II does not coat the glass surface and it binds to spermatozoa. Data are consistent with the view that ASF-II has not been derived from the larger ASF-I molecule due to its enzymic modifications. Both ASF-I and -II had no effect on sperm forward motility as evidenced by spectrophotometric motility assays, indicating thereby the suitability of the factors to improve the existing sperm motility assays by eliminating the possibility of cell-sticking artifacts.
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PMID:Characterization of anti-sticking factor-II from goat epididymal plasma. 209 69

Several lines of evidence have demonstrated conclusively the presence of cAMP-dependent protein kinase (ecto-RC) activity on the external surface of goat cauda-epididymal intact spermatozoa. The intact-cell ecto-kinase that caused transfer of the terminal phosphate of exogenous ATP to the serine and threonine residues of exogenous histone was specifically activated by cAMP. As well, the ecto-kinase caused phosphorylation of the synthetic peptide Kemptide. The isolated spermatozoa, before or after incubation with reaction mixture for ecto-kinase assays, were approximately 99.5% viable, as shown by the analyses of ethidium bromide fluorescence and the cytosolic marker enzymes lactic dehydrogenase and 3-phosphoglycerate kinase. The ecto-kinase activity was not due to contamination of epididymal plasma and damaged cells or to protein kinase that may have leaked from the cells. There was little uptake of ATP and histone by the cells. The intact-cell kinase activity was strongly (80-90%) inhibited by treatment with membrane nonpenetrating surface probes: p-chloromercuriphenylsulfonic acid (2 microM), diazonium salt of sulfanilic acid (DSS, 0.5 mM), and proteases such as trypsin, chymotrypsin, and pronase (each 125 micrograms/mL). Disruption of sperm plasma membrane by sonication or Triton X-100 (0.2%) caused about a fivefold increase of the intact sperm kinase activity. Highly purified sperm plasma membrane (PM) possessed ecto-kinase activity that was resolved into type I and II kinases by DEAE-cellulose chromatography, the type I isoenzyme being the major (approximately 70%) enzymic species. Treatment of the intact spermatozoa with DSS prior to isolation of PM caused a marked loss of the activities of both the isoenzymes, indicating thereby the "ecto" nature of the PM-bound type I and II kinases. Preparations of vigorously forward-motile spermatozoa with 100% intactness had approximately fourfold higher specific activity of the ecto-kinase than the "composite" cells from which the former cells were isolated. However, the profiles of the type I and II ecto-kinases of the composite, as well as forward-motile spermatozoa, were nearly identical. The data are consistent with the view that ecto-kinases may have role in the regulation of flagellar motility.
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PMID:Type I and II cAMP-dependent ecto-protein kinases in goat epididymal spermatozoa and their enriched activities in forward-motile spermatozoa. 216 Aug 33

N-acetyl-beta-D-glucosaminidase from human seminal plasma has been separated by the cellulose acetate electrophoresis into two components, isoenzyme I and II. The two isoenzymes are readily separated on a DEAE-Sephadex column. Isoenzyme I which has adsorbed to the column, is eluted at 0.1 M NaCl, whereas isoenzyme II has passed through the column. The following enzyme properties have been obtained: 1) Both isoenzymes show the same Km values (0.27 X 10(-3) M) towards sodio-m-cresol-sufonphtaleinyl-N-acetyl-beta-D-glucosaminide . 2) Both isoenzymes show the same pH optima of 5.4. 3) Optimal temperature for isoenzyme I is 50 degrees C, while that for isoenzyme II is 65 degrees C. Isoenzyme II is heat stable, while isoenzyme I is easily denatured by heat. These characteristics of isoenzyme I and II coincide with previous reports of NAG A and B from the spleen and the kidney, respectively. The activity ratio of isoenzyme I and II has been studied for the reproductive tissues. The % ratio of isoenzyme I and II in the epididymal head is 62 and 38, that in the epididymal tail is 42 and 58, and 38:62 in the seminal vesicle, 35:65 in the prostatic gland and 27:73 in the seminal plasma.
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PMID:[Separation and properties of N-acetyl-beta-D-glucosaminidase from human seminal plasma]. 259 37

1. Ram seminal plasma alpha-glucosidase has been purified in order to increase our knowledge of this enzyme and of its role in epididymal physiology. 2. Since the enzyme behaved differently from other known acid alpha-glucosidases and was not affinity-adsorbed on dextran gels, another approach had to be used. 3. The final procedure included an ethanol precipitation step, sequential chromatography on hydroxylapatite and DEAE Sepharose CL-6B, isoelectric focusing in polyacrylamide gels and ultrafiltration. 4. The resulting purification factor of alpha-glucosidase was 9822 with an overall yield of 5%. 5. The purified material consisted of several isoforms with a mol. wt of 105,000 and isoelectric points varying between 4 and 5.
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PMID:Purification of ram seminal plasma acid alpha-glucosidase. 312 30


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