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Volumn 11, Issue 6, 1999, Pages 379-386

Partial purification and characterization of a phosphoprotein phosphatase from sperm plasma membrane

Author keywords

External cell surface protein dephosphorylation; Goat; Spermatozoa

Indexed keywords

CONCANAVALIN A; DETERGENT; FLUORIDE SODIUM; GLYCOPROTEIN; LACTOPEROXIDASE; ORTHOVANADIC ACID; PHOSPHATE; POLYSORBATE 20; PYROPHOSPHATE; SODIUM HYDROXIDE; SPERMIDINE; SPERMINE; TYLOXAPOL;

EID: 0033366054     PISSN: 10313613     EISSN: None     Source Type: Journal    
DOI: 10.1071/RD99095     Document Type: Article
Times cited : (9)

References (61)
  • 1
    • 0031560923 scopus 로고    scopus 로고
    • Regulation of fowl sperm flagellar motility by protein phosphatase type I and its relationship with dephosphorylation of axonemal and/or accessory cytoskeletal proteins
    • Ashizawa, K., Hashimoto, K., and Tsuzuki, Y. (1997). Regulation of fowl sperm flagellar motility by protein phosphatase Type I and its relationship with dephosphorylation of axonemal and/or accessory cytoskeletal proteins. Biochem. Biophys. Res. Commun. 235, 108-12.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 108-112
    • Ashizawa, K.1    Hashimoto, K.2    Tsuzuki, Y.3
  • 2
    • 0023377086 scopus 로고
    • Enzymatic characteristics of ecto-phosphoprotein phosphatase in goat epididymal intact spermatozoa
    • Barua, M., and Majumder, G. C. (1987). Enzymatic characteristics of ecto-phosphoprotein phosphatase in goat epididymal intact spermatozoa. Biochem. Cell Biol. 65, 602-9.
    • (1987) Biochem. Cell Biol. , vol.65 , pp. 602-609
    • Barua, M.1    Majumder, G.C.2
  • 3
    • 0021894990 scopus 로고
    • Occurrence of an ecto-phosphoprotein phosphatase in goat epididymal spermatozoa
    • Barua, M., Bhattacharyya, U., and Majumder, G. C. (1985). Occurrence of an ecto-phosphoprotein phosphatase in goat epididymal spermatozoa. Biochem. Int. 10, 733-41.
    • (1985) Biochem. Int. , vol.10 , pp. 733-741
    • Barua, M.1    Bhattacharyya, U.2    Majumder, G.C.3
  • 4
    • 0025301776 scopus 로고
    • Occurrence of a coupled-enzyme system on the intact-sperm outer surface that phosphorylates and dephosphoryiates ecto-proteins
    • Barua, M., Haldar, S., and Majumder, G. C. (1990). Occurrence of a coupled-enzyme system on the intact-sperm outer surface that phosphorylates and dephosphoryiates ecto-proteins. Biochem. Int. 20, 1089-96.
    • (1990) Biochem. Int. , vol.20 , pp. 1089-1096
    • Barua, M.1    Haldar, S.2    Majumder, G.C.3
  • 5
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Bensadoun, A., and Weinstein, D. (1976). Assay of proteins in the presence of interfering materials. Anal. Biochem. 70, 241-50.
    • (1976) Anal. Biochem. , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 6
    • 0023739108 scopus 로고
    • Protein kinases: A current perspective
    • Blackshear, P. J., Nairn, A. C., and Kuo, J. F. (1988). Protein kinases: a current perspective. FASEB J. 2, 2957-69.
    • (1988) FASEB J. , vol.2 , pp. 2957-2969
    • Blackshear, P.J.1    Nairn, A.C.2    Kuo, J.F.3
  • 7
    • 0018830277 scopus 로고
    • A cAMP-dependent phosphorylated motility protein in bovine epididymal sperm
    • Brandt, H., and Hoskins, D. D. (1980). A cAMP-dependent phosphorylated motility protein in bovine epididymal sperm. J. Biol. Chem. 255, 982-7.
    • (1980) J. Biol. Chem. , vol.255 , pp. 982-987
    • Brandt, H.1    Hoskins, D.D.2
  • 8
    • 0019320478 scopus 로고
    • Phosphorylase phosphatase complex from skeletal muscle: Activation of one of two catalytic subunits by manganese ions
    • Brautigan, D. L., Picton, C., and Fischer, E. H. (1980). Phosphorylase phosphatase complex from skeletal muscle: Activation of one of two catalytic subunits by manganese ions. Biochemistry 19, 5787-94.
    • (1980) Biochemistry , vol.19 , pp. 5787-5794
    • Brautigan, D.L.1    Picton, C.2    Fischer, E.H.3
  • 9
    • 0023440964 scopus 로고
    • Regulation of sperm flagellar motility by calcium and cAMP-dependent phosphorylation
    • Brokaw, C. J. (1987). Regulation of sperm flagellar motility by calcium and cAMP-dependent phosphorylation. J. Cell Biochem. 35, 175-184
    • (1987) J. Cell Biochem. , vol.35 , pp. 175-184
    • Brokaw, C.J.1
  • 10
    • 0021794328 scopus 로고
    • Calcium-dependent association of a protein complex with the lymphocyte plasma membrane: Probable identity with calmodulin-calcineurin
    • Chantier, P. D. (1985). Calcium-dependent association of a protein complex with the lymphocyte plasma membrane: probable identity with calmodulin-calcineurin. J. Cell Biol. 101, 207-16.
    • (1985) J. Cell Biol. , vol.101 , pp. 207-216
    • Chantier, P.D.1
  • 11
    • 0019982538 scopus 로고
    • The role of protein phosphorylation in neural and hormonal control of cellular activity
    • Cohen, P. (1982). The role of protein phosphorylation in neural and hormonal control of cellular activity. Nature 296, 613-20.
    • (1982) Nature , vol.296 , pp. 613-620
    • Cohen, P.1
  • 12
    • 0019332824 scopus 로고
    • Purification and properties of eIF-2 phosphatase
    • Crouch, D., and Safer, B. (1980). Purification and properties of eIF-2 phosphatase. J. Biol. Chem. 255, 7918-24.
    • (1980) J. Biol. Chem. , vol.255 , pp. 7918-7924
    • Crouch, D.1    Safer, B.2
  • 13
    • 0023892708 scopus 로고
    • Endogenous hyperphosphorylation in plasma membrane from an ascites hepatocarcinoma cell line
    • Church, J. G., Ghosh, S., Roufogalis, B. D., and Villabo, A. (1988). Endogenous hyperphosphorylation in plasma membrane from an ascites hepatocarcinoma cell line. Biochem. Cell Biol. 66, 1-12.
    • (1988) Biochem. Cell Biol. , vol.66 , pp. 1-12
    • Church, J.G.1    Ghosh, S.2    Roufogalis, B.D.3    Villabo, A.4
  • 14
    • 1842301114 scopus 로고    scopus 로고
    • A maturation-related differential phosphorylation of plasma membrane proteins of the epididymal spermatozoa of the hamster by endogenous protein kinase
    • Devi, K. U., Ahmad, M. B., and Shivaji, S. (1997). A maturation-related differential phosphorylation of plasma membrane proteins of the epididymal spermatozoa of the hamster by endogenous protein kinase. Mol. Reprod. Dev. 47, 341-50.
    • (1997) Mol. Reprod. Dev. , vol.47 , pp. 341-350
    • Devi, K.U.1    Ahmad, M.B.2    Shivaji, S.3
  • 15
    • 0345643446 scopus 로고    scopus 로고
    • Plasma membrane-associated protein tyrosine phosphatase activity in hamster spermatozoa
    • Devi, K. U., Jha, K., and Shivaji, S. (1999). Plasma membrane-associated protein tyrosine phosphatase activity in hamster spermatozoa. Mol. Reprod. Dev. 33, 42-50.
    • (1999) Mol. Reprod. Dev. , vol.33 , pp. 42-50
    • Devi, K.U.1    Jha, K.2    Shivaji, S.3
  • 16
    • 0023789664 scopus 로고
    • A simple quantitative method of estimation of cell intactness based on ethidium bromide fluorescence
    • Dey, C. S., and Majumder G. C. (1988). A simple quantitative method of estimation of cell intactness based on ethidium bromide fluorescence. Biochem. Int. 17, 367-74.
    • (1988) Biochem. Int. , vol.17 , pp. 367-374
    • Dey, C.S.1    Majumder, G.C.2
  • 17
    • 0019503917 scopus 로고
    • Dephosphorylation of rabbit skeleton muscle phosphorylase kinase: Evidence against the operation of the second-site phosphorylation mechanism of regulation
    • Ganapathi, M. K., Silberman, S. R., Paris, H., and Lee, E.V. C. (1981). Dephosphorylation of rabbit skeleton muscle phosphorylase kinase: Evidence against the operation of the second-site phosphorylation mechanism of regulation. J. Biol. Chem. 256, 3213-17.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3213-3217
    • Ganapathi, M.K.1    Silberman, S.R.2    Paris, H.3    Lee, E.V.C.4
  • 19
    • 0025353128 scopus 로고
    • Hepatic protein kinase-C and protein phosphatase type 2A in the fetal rat
    • Gruppuso, P. A. (1990). Hepatic protein kinase-C and protein phosphatase type 2A in the fetal rat. Pediatr. Res. 27, 599-603.
    • (1990) Pediatr. Res. , vol.27 , pp. 599-603
    • Gruppuso, P.A.1
  • 20
    • 0021326549 scopus 로고
    • Intrinsic phosphatase activity of bovine brain calcineurin requires a tightly bound trace metal
    • Gupta, R. C., Khandelwal, R. L., and Sulakhe, P. V. (1984). Intrinsic phosphatase activity of bovine brain calcineurin requires a tightly bound trace metal. FEBS Lett. 169, 251-5.
    • (1984) FEBS Lett. , vol.169 , pp. 251-255
    • Gupta, R.C.1    Khandelwal, R.L.2    Sulakhe, P.V.3
  • 21
    • 0022443368 scopus 로고
    • Phosphorylation of external cell surface proteins by an endogenous ecto-protein kinase of goat epididymal intact spermatozoa
    • Haldar, S., and Majumder, G. C. (1986). Phosphorylation of external cell surface proteins by an endogenous ecto-protein kinase of goat epididymal intact spermatozoa. Biochim. Biophys. Acta 887, 291-303.
    • (1986) Biochim. Biophys. Acta , vol.887 , pp. 291-303
    • Haldar, S.1    Majumder, G.C.2
  • 22
    • 0022975648 scopus 로고
    • An ecto-cyclic AMP-independent protein kinase in goat spermatozoa and its change of activity during forward motility
    • Haldar S., Dey, C. S., and Majumder, G. C. (1986). An ecto-cyclic AMP-independent protein kinase in goat spermatozoa and its change of activity during forward motility. Biochem. Int. 13, 809-17.
    • (1986) Biochem. Int. , vol.13 , pp. 809-817
    • Haldar, S.1    Dey, C.S.2    Majumder, G.C.3
  • 23
    • 0026045230 scopus 로고
    • Okadaic acid-induced inhibition of B-50 dephosphorylation by presynaptic membrane-associated protein phosphatases
    • Han, Y. F., and Dokas, L. A. (1991). Okadaic acid-induced inhibition of B-50 dephosphorylation by presynaptic membrane-associated protein phosphatases. J. Neurochem. 57, 1325-31.
    • (1991) J. Neurochem. , vol.57 , pp. 1325-1331
    • Han, Y.F.1    Dokas, L.A.2
  • 25
    • 0016434852 scopus 로고
    • Externally disposed plasma membrane proteins
    • Hubbard, A. L., and Cohn, Z. A. (1975). Externally disposed plasma membrane proteins. J. Cell Biol. 64, 438-60.
    • (1975) J. Cell Biol. , vol.64 , pp. 438-460
    • Hubbard, A.L.1    Cohn, Z.A.2
  • 26
    • 0020565637 scopus 로고
    • Protein phosphatases: Properties and role in cellular regulation
    • Ingebitsen, T. S., and Cohen, P. (1983). Protein phosphatases: properties and role in cellular regulation. Science 221, 331-8.
    • (1983) Science , vol.221 , pp. 331-338
    • Ingebitsen, T.S.1    Cohen, P.2
  • 27
    • 0017688786 scopus 로고
    • Some properties of purified phosphoprotein phosphatases from rabbit liver
    • Khandelwal, R. L. (1977). Some properties of purified phosphoprotein phosphatases from rabbit liver. Biochim. Biophys. Acta 485, 379-90.
    • (1977) Biochim. Biophys. Acta , vol.485 , pp. 379-390
    • Khandelwal, R.L.1
  • 28
    • 0028593413 scopus 로고
    • A membrane-bound protein phosphatase type 2C from Paramecium tetraurelia: Purification, characterization and cloning
    • Klumpp, S., Hanke, C., Donella-Deana, A., Beyer, A., Kellner, R., Pinna, L. A., and Schuttz, J. E. (1994). A membrane-bound protein phosphatase type 2C from Paramecium tetraurelia: Purification, characterization and cloning. J. Biol. Chem. 269, 32774-80.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32774-32780
    • Klumpp, S.1    Hanke, C.2    Donella-Deana, A.3    Beyer, A.4    Kellner, R.5    Pinna, L.A.6    Schuttz, J.E.7
  • 29
    • 0019412054 scopus 로고
    • Phosphoprotein phosphatase associated with rat liver plasma membrane: Properties of phosphorylase phosphatase and phosphohistone phosphatase
    • Kobayashi, M., and Ozawa, T. (1981). Phosphoprotein phosphatase associated with rat liver plasma membrane: Properties of phosphorylase phosphatase and phosphohistone phosphatase. J. Biochem. 89, 731-40.
    • (1981) J. Biochem. , vol.89 , pp. 731-740
    • Kobayashi, M.1    Ozawa, T.2
  • 30
    • 0020084899 scopus 로고
    • Protein kinase activity and substrates at the surface of intact HeLa cells
    • Kubler, D., Pyerin, W., and Kinzel, V. (1982). Protein kinase activity and substrates at the surface of intact HeLa cells. J. Biol. Chem. 257, 322-9.
    • (1982) J. Biol. Chem. , vol.257 , pp. 322-329
    • Kubler, D.1    Pyerin, W.2    Kinzel, V.3
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature, 227, 680-85.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0017880056 scopus 로고
    • Purification and properties of phosphoprotein phosphatases with different substrate and divalent cation specificities from canine heart
    • Li, H. C., Hsiao, K. Y., and Chan, W. W. S. (1978). Purification and properties of phosphoprotein phosphatases with different substrate and divalent cation specificities from canine heart. Eur. J. Biochem. 84, 215-25.
    • (1978) Eur. J. Biochem. , vol.84 , pp. 215-225
    • Li, H.C.1    Hsiao, K.Y.2    Chan, W.W.S.3
  • 34
    • 0025860032 scopus 로고
    • Phosphotyrosyl turnover in insulin signalling. Characterization of two membrane-bound pp15 protein tyrosine phosphatases from 3T3-L1 adipocytes
    • Liao, K., Hoffman, R. D., and Lane, M. D. (1991). Phosphotyrosyl turnover in insulin signalling. Characterization of two membrane-bound pp15 protein tyrosine phosphatases from 3T3-L1 adipocytes. J. Biol. Chem. 266, 6544-53.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6544-6553
    • Liao, K.1    Hoffman, R.D.2    Lane, M.D.3
  • 36
    • 0015523042 scopus 로고
    • Phosphoprotein phosphatases from rat cerebral cortex: Subcellular distribution and characterization
    • Maeno, H., and Greengard, P. (1972). Phosphoprotein phosphatases from rat cerebral cortex: Subcellular distribution and characterization. J. Biol. Chem. 247, 3269-77.
    • (1972) J. Biol. Chem. , vol.247 , pp. 3269-3277
    • Maeno, H.1    Greengard, P.2
  • 37
    • 0015524077 scopus 로고
    • Hormone dependent phosphorylation of ribosomal and plasma membrane proteins in mouse mammary gland in vitro
    • Majumder, G. C., and Turkington, R. W. (1972). Hormone dependent phosphorylation of ribosomal and plasma membrane proteins in mouse mammary gland in vitro. J. Biol. Chem. 247, 7207-17.
    • (1972) J. Biol. Chem. , vol.247 , pp. 7207-7217
    • Majumder, G.C.1    Turkington, R.W.2
  • 38
    • 84907123526 scopus 로고
    • Biochemical parameters of initiation and regulation of sperm motility
    • Majumder, G. C., Dey, C. S., Haldar, S., and Barua, M. (1990). Biochemical parameters of initiation and regulation of sperm motility. Arch. Androl. 24, 287-303.
    • (1990) Arch. Androl. , vol.24 , pp. 287-303
    • Majumder, G.C.1    Dey, C.S.2    Haldar, S.3    Barua, M.4
  • 40
    • 0018422880 scopus 로고
    • Phosphoprotein phosphatase activity at the outer surface of intact normal and transformed 3T3 fibroblasts
    • Makan, N. R. (1979). Phosphoprotein phosphatase activity at the outer surface of intact normal and transformed 3T3 fibroblasts. Biochim. Biophys. Acta 585, 360-73.
    • (1979) Biochim. Biophys. Acta , vol.585 , pp. 360-373
    • Makan, N.R.1
  • 41
    • 0014690970 scopus 로고
    • Characterization of a phosphatase specific for phosphorylated histones and protamine
    • Meisler, M. H., and Langan, T. A. (1969). Characterization of a phosphatase specific for phosphorylated histones and protamine. J. Biol. Chem. 244, 4961-8.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4961-4968
    • Meisler, M.H.1    Langan, T.A.2
  • 42
    • 0028441515 scopus 로고
    • Purification and characterization of a protein kinase from goat sperm plasma membrane
    • Mitra S., Nath, D., and Majumder, G. C. (1994). Purification and characterization of a protein kinase from goat sperm plasma membrane. Biochem. Cell. Biol. 72, 218-26.
    • (1994) Biochem. Cell. Biol. , vol.72 , pp. 218-226
    • Mitra, S.1    Nath, D.2    Majumder, G.C.3
  • 43
    • 0033041652 scopus 로고    scopus 로고
    • Maturation-dependent modification of the protein phosphorylation profile of isolated goat sperm plasma membrane
    • Nath, D., and Majumder, G. C. (1999). Maturation-dependent modification of the protein phosphorylation profile of isolated goat sperm plasma membrane. J. Reprod. Fertil. 115, 29-37.
    • (1999) J. Reprod. Fertil. , vol.115 , pp. 29-37
    • Nath, D.1    Majumder, G.C.2
  • 44
    • 0021195602 scopus 로고
    • Protein phosphorylation of plasma membranes from bovine epididymal spermatozoa
    • Noland, T. D., Olson, G. E., and Garbers, D. L. (1984). Protein phosphorylation of plasma membranes from bovine epididymal spermatozoa. Biol. Reprod. 31, 185-94.
    • (1984) Biol. Reprod. , vol.31 , pp. 185-194
    • Noland, T.D.1    Olson, G.E.2    Garbers, D.L.3
  • 45
    • 0019332717 scopus 로고
    • Dephosphorylation of the 20,000 dalton light chain of myosin by two different phosphatases from smooth muscle
    • Pato, M. D., and Adelstein, R. S. (1980). Dephosphorylation of the 20,000 dalton light chain of myosin by two different phosphatases from smooth muscle. J. Biol. Chem. 255, 6535-8.
    • (1980) J. Biol. Chem. , vol.255 , pp. 6535-6538
    • Pato, M.D.1    Adelstein, R.S.2
  • 46
    • 0023083272 scopus 로고
    • Factors influencing the yield and purity of goat sperm plasma membranes isolated by means of an aqueous two-phase polymer system
    • Rana, A. P. S., and Majumder, G. C. (1987). Factors influencing the yield and purity of goat sperm plasma membranes isolated by means of an aqueous two-phase polymer system. Prep. Biochem. 17, 261-81.
    • (1987) Prep. Biochem. , vol.17 , pp. 261-281
    • Rana, A.P.S.1    Majumder, G.C.2
  • 47
    • 0014754275 scopus 로고
    • An evaluation of film detection methods for weak β-emitters, particularly tritium
    • Randerath, K. (1970). An evaluation of film detection methods for weak β-emitters, particularly tritium. Anal. Biochem. 34, 188-205.
    • (1970) Anal. Biochem. , vol.34 , pp. 188-205
    • Randerath, K.1
  • 48
    • 0015933309 scopus 로고
    • The role of cyclic AMP in the phosphorylation of proteins in human erytrocyte membranes
    • Rubin, C. S., and Rosen, O. M. (1973). The role of cyclic AMP in the phosphorylation of proteins in human erytrocyte membranes. Biochem. Biophys. Res. Commun. 50, 421-9.
    • (1973) Biochem. Biophys. Res. Commun. , vol.50 , pp. 421-429
    • Rubin, C.S.1    Rosen, O.M.2
  • 49
    • 49049147925 scopus 로고
    • Cyclic AMP dependent protein phosphorylation on the surface of rat hepatocytes
    • Sommarin, M. Henriksson, T., and Jergil, B. (1981). Cyclic AMP dependent protein phosphorylation on the surface of rat hepatocytes. FEBS Lett. 127, 285-9.
    • (1981) FEBS Lett. , vol.127 , pp. 285-289
    • Sommarin, M.1    Henriksson, T.2    Jergil, B.3
  • 51
    • 0019974782 scopus 로고
    • Phosphoprotein phosphatase activity of sea urchin spermatozoa
    • Swarup, G., and Garbers, D. L. (1982). Phosphoprotein phosphatase activity of sea urchin spermatozoa. Biol. Reprod. 26, 953-60.
    • (1982) Biol. Reprod. , vol.26 , pp. 953-960
    • Swarup, G.1    Garbers, D.L.2
  • 52
    • 0015214590 scopus 로고
    • Phosphoprotein kinases associated with rat liver chromatin
    • Takeda, M., Yamamura, H., and Ohga, Y. (1971). Phosphoprotein kinases associated with rat liver chromatin. Biachem. Biophys. Res. Commun. 42, 103-10.
    • (1971) Biachem. Biophys. Res. Commun. , vol.42 , pp. 103-110
    • Takeda, M.1    Yamamura, H.2    Ohga, Y.3
  • 53
    • 0022536347 scopus 로고
    • Axokinin phosphorylation by cAMP-dependent protein kinase is sufficient for activation of sperm flagellar motility
    • Tash, J. S., Hidaka, H., and Means, A. R. (1986). Axokinin phosphorylation by cAMP-dependent protein kinase is sufficient for activation of sperm flagellar motility. J. Cell Biol. 103, 649-55.
    • (1986) J. Cell Biol. , vol.103 , pp. 649-655
    • Tash, J.S.1    Hidaka, H.2    Means, A.R.3
  • 54
    • 0023952125 scopus 로고
    • Identification, characterization and functional correlation of calmodulin-dependent protein phosphatase in sperm
    • Tash J. S., Krinks, M., Patel, J., Means, R. L., Klee, C. B., and Means, A. R. (1988). Identification, characterization and functional correlation of calmodulin-dependent protein phosphatase in sperm. J. Cell Biol. 106, 1625-33.
    • (1988) J. Cell Biol. , vol.106 , pp. 1625-1633
    • Tash, J.S.1    Krinks, M.2    Patel, J.3    Means, R.L.4    Klee, C.B.5    Means, A.R.6
  • 55
    • 0021380513 scopus 로고
    • The catalytic subunits of protein phosphatase-1 and protein phosphatase-2A are distinct gene product
    • Tung, H. Y. L., Resink, T. J., Hammings, B. A., Shenolikar, S., and Cohen, P. (1984). The catalytic subunits of protein phosphatase-1 and protein phosphatase-2A are distinct gene product. Eur. J. Biochem. 138, 635-41.
    • (1984) Eur. J. Biochem. , vol.138 , pp. 635-641
    • Tung, H.Y.L.1    Resink, T.J.2    Hammings, B.A.3    Shenolikar, S.4    Cohen, P.5
  • 56
    • 0013668878 scopus 로고
    • Dephosphorylation of a major sperm membrane protein is induced by egg jelly during sea urchin fertilization
    • Ward, G. E., and Vacquier, V. D. (1983). Dephosphorylation of a major sperm membrane protein is induced by egg jelly during sea urchin fertilization. Proc. Natl Acad. Sci. USA 80, 5578-82.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 5578-5582
    • Ward, G.E.1    Vacquier, V.D.2
  • 57
    • 0347133977 scopus 로고
    • The physiological regulation and function of cAMP-dependent protein kinase
    • Walsh, D. A., and Cooper, R. H. (1979). The physiological regulation and function of cAMP-dependent protein kinase. Biochem. Actions Horm. 6, 1-75.
    • (1979) Biochem. Actions Horm. , vol.6 , pp. 1-75
    • Walsh, D.A.1    Cooper, R.H.2
  • 58
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by Dodecyl Sulfate polyacrylamide gel electrophoresis
    • Weber, K., and Osborn, M. (1969). The reliability of molecular weight determinations by Dodecyl Sulfate polyacrylamide gel electrophoresis. J. Biol. Chem. 244, 4406-12.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 59
    • 0019882018 scopus 로고
    • Silver staining of proteins in polyacrylamide gels
    • Wray, W., Banlikas, T., Wray, V. P., and Hancock, R. (1981). Silver staining of proteins in polyacrylamide gels. Anal. Biochem. 118, 197-203.
    • (1981) Anal. Biochem. , vol.118 , pp. 197-203
    • Wray, W.1    Banlikas, T.2    Wray, V.P.3    Hancock, R.4
  • 60
    • 0025820738 scopus 로고
    • Membrane-bound phosphotyrosine phosphatases
    • Williams, A. F. (1991). Membrane-bound phosphotyrosine phosphatases. Science 252, 764.
    • (1991) Science , vol.252 , pp. 764
    • Williams, A.F.1
  • 61
    • 0026556671 scopus 로고
    • The mechanism of activation of protein kinase FA (the activator of type-I protein phosphatase) in brain synaptosomes
    • Yang, SD, Yu, J. S., Fong, Y. L., and Liu, J. S. (1992). The mechanism of activation of protein kinase FA (the activator of type-I protein phosphatase) in brain synaptosomes. Biochem. Biophys. Res. Commun. 182, 129-36.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 129-136
    • Yang, S.D.1    Yu, J.S.2    Fong, Y.L.3    Liu, J.S.4


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