메뉴 건너뛰기




Volumn 119, Issue 3, 1998, Pages 571-576

Purification and properties of embryonic cysteine proteinase which participates in yolk-lysis of Xenopus laevis

Author keywords

Amino acid sequence; Antibody; Cysteine proteinase; Embryo; Inhibitor; Purification; Xenopus laevis; Yolk lysis

Indexed keywords

CATHEPSIN B; CYSTEINE PROTEINASE;

EID: 0031903727     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(98)00030-3     Document Type: Article
Times cited : (16)

References (28)
  • 1
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H, cathepsin L
    • Barrett AJ, Kirschke H. Cathepsin B, cathepsin H, cathepsin L. Methods Enzymol 1981;80:535-61.
    • (1981) Methods Enzymol , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 2
    • 0015890981 scopus 로고
    • Staining of phospho-proteins on acrylamide gel electropherograms
    • Cutting JA, Roth TF. Staining of phospho-proteins on acrylamide gel electropherograms. Anal Biochem 1973;54:386-94.
    • (1973) Anal Biochem , vol.54 , pp. 386-394
    • Cutting, J.A.1    Roth, T.F.2
  • 3
    • 0029128688 scopus 로고
    • Avian cathepsin B cDNA: Sequence and demonstration that mRNAs of 2 sizes are produced in cell types producing large quantities of the enzyme
    • Dong S-S, Stransky GI, Whitaker CH, Jordan SE, Schlesinger PH, Edwards JC, Blair HC. Avian cathepsin B cDNA: Sequence and demonstration that mRNAs of 2 sizes are produced in cell types producing large quantities of the enzyme. Biochim Biophys Acta 1995;1251:69-73.
    • (1995) Biochim Biophys Acta , vol.1251 , pp. 69-73
    • Dong, S.-S.1    Stransky, G.I.2    Whitaker, C.H.3    Jordan, S.E.4    Schlesinger, P.H.5    Edwards, J.C.6    Blair, H.C.7
  • 4
    • 0345815365 scopus 로고
    • The breakdown of isolated yolk granules by cations
    • Essner ES. The breakdown of isolated yolk granules by cations. Protoplasma 1954;43:79-89.
    • (1954) Protoplasma , vol.43 , pp. 79-89
    • Essner, E.S.1
  • 5
    • 0028587431 scopus 로고
    • Changes in yolk platelet pH during Xenopus laevis development correlate with yolk utilization
    • Fagotto F, Maxfield FR. Changes in yolk platelet pH during Xenopus laevis development correlate with yolk utilization. J Cell Sci 1994;107:3325-37.
    • (1994) J Cell Sci , vol.107 , pp. 3325-3337
    • Fagotto, F.1    Maxfield, F.R.2
  • 6
    • 0023926852 scopus 로고
    • Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H
    • Fuchs R, Machleidt W, Gassen HG. Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H. Biol Chem Hoppe-Seyler 1988;369:469-75.
    • (1988) Biol Chem Hoppe-Seyler , vol.369 , pp. 469-475
    • Fuchs, R.1    Machleidt, W.2    Gassen, H.G.3
  • 7
    • 0024008084 scopus 로고
    • Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L
    • Joseph LJ, Chang LC, Stamenkovich D, Sukhatme VP. Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. J Clin Invest 1988;81:1621-9.
    • (1988) J Clin Invest , vol.81 , pp. 1621-1629
    • Joseph, L.J.1    Chang, L.C.2    Stamenkovich, D.3    Sukhatme, V.P.4
  • 8
    • 0025059406 scopus 로고
    • Purification and characterization of a cysteine proteinase from silkworm eggs
    • Kageyama T, Takahashi SY. Purification and characterization of a cysteine proteinase from silkworm eggs. Eur J Biochem 1990;193:203-10.
    • (1990) Eur J Biochem , vol.193 , pp. 203-210
    • Kageyama, T.1    Takahashi, S.Y.2
  • 11
    • 0024218968 scopus 로고
    • Characterization of proteolytic activities in embryos of Xenopus laevis
    • Miyata S, Kihara HK. Characterization of proteolytic activities in embryos of Xenopus laevis. Comp Biochem Physiol 1988;91B:651-6.
    • (1988) Comp Biochem Physiol , vol.91 B , pp. 651-656
    • Miyata, S.1    Kihara, H.K.2
  • 12
    • 0029556715 scopus 로고
    • Kihara HK Cathepsin L-like protease from Xenopus embryos that is stimulated by nucleoside phosphates and nucleic acids
    • Miyata S, Kihara HK Cathepsin L-like protease from Xenopus embryos that is stimulated by nucleoside phosphates and nucleic acids. Zool Sci 1995;12:771-4.
    • (1995) Zool Sci , vol.12 , pp. 771-774
    • Miyata, S.1
  • 13
    • 0029005298 scopus 로고
    • Effects on properties of a thiol protease from Xenopus embryos of changes in substrate and assay conditions
    • Miyata S, Nishibe Y, Kihara HK. Effects on properties of a thiol protease from Xenopus embryos of changes in substrate and assay conditions. Cell Biol Int 1995;19:333-8.
    • (1995) Cell Biol Int , vol.19 , pp. 333-338
    • Miyata, S.1    Nishibe, Y.2    Kihara, H.K.3
  • 15
    • 0024803003 scopus 로고
    • Purification and characterization of a protease from Xenopus embryos
    • Miyata S, Yoshida Y, Kihara HK. Purification and characterization of a protease from Xenopus embryos. Eur J Biochem 1989;186:49-54.
    • (1989) Eur J Biochem , vol.186 , pp. 49-54
    • Miyata, S.1    Yoshida, Y.2    Kihara, H.K.3
  • 16
    • 0345815364 scopus 로고
    • Required salt concentration for successful fertilization of Xenopus laevis
    • Moriya M. Required salt concentration for successful fertilization of Xenopus laevis. J Fac Sci Hokkaido Univ Ser VI 1976;20:272-6.
    • (1976) J Fac Sci Hokkaido Univ Ser VI , vol.20 , pp. 272-276
    • Moriya, M.1
  • 17
    • 0028973519 scopus 로고
    • Characterization of gene of anuran cathepsin D as a metamorphosis-associated enzyme
    • Mukai M, Obara M, Yoshizato K Characterization of gene of anuran cathepsin D as a metamorphosis-associated enzyme. Dev Growth Differ 1995;37:463-77.
    • (1995) Dev Growth Differ , vol.37 , pp. 463-477
    • Mukai, M.1    Obara, M.2    Yoshizato, K.3
  • 18
    • 0029936001 scopus 로고    scopus 로고
    • Vitellogenesis-related ovary cathepsin D from Xenopus laevis: Purification and properties in comparison with liver cathepsin D
    • Nakamura K, Yonezawa S, Yoshizaki N. Vitellogenesis-related ovary cathepsin D from Xenopus laevis: Purification and properties in comparison with liver cathepsin D. Comp Biochem Physiol 1996; 113B:835-40.
    • (1996) Comp Biochem Physiol , vol.113 B , pp. 835-840
    • Nakamura, K.1    Yonezawa, S.2    Yoshizaki, N.3
  • 21
    • 0028095918 scopus 로고
    • Involvement of the lysosomal system in yolk protein deposit and degradation during vitellogenesis and embryonic development in trout
    • Sire MF, Babin PJ, Vernier JM. Involvement of the lysosomal system in yolk protein deposit and degradation during vitellogenesis and embryonic development in trout. J Exp Zool 1994;269:69-83.
    • (1994) J Exp Zool , vol.269 , pp. 69-83
    • Sire, M.F.1    Babin, P.J.2    Vernier, J.M.3
  • 23
    • 0027177631 scopus 로고
    • Cysteine proteinase from the eggs of the silkmoth, Bombyx mori: Identification of a latent enzyme and characterization of activation and proteolytic processing in vivo and in vitro
    • Takahashi SY, Yamamoto Y, Shinoya Y, Kageyama T. Cysteine proteinase from the eggs of the silkmoth, Bombyx mori: Identification of a latent enzyme and characterization of activation and proteolytic processing in vivo and in vitro. J Biochem 1993;114:267-72.
    • (1993) J Biochem , vol.114 , pp. 267-272
    • Takahashi, S.Y.1    Yamamoto, Y.2    Shinoya, Y.3    Kageyama, T.4
  • 24
    • 0001573128 scopus 로고
    • Acid cysteine proteinase from the eggs of silkmoth, Bombyx mori: Tissue distribution, developmental changes and the sites of synthesis for the enzyme
    • Takahashi SY, Zhao X, Kageyama T, Yamamoto Y. Acid cysteine proteinase from the eggs of silkmoth, Bombyx mori: Tissue distribution, developmental changes and the sites of synthesis for the enzyme. Insect Biochem Mol Biol 1992;22:369-77.
    • (1992) Insect Biochem Mol Biol , vol.22 , pp. 369-377
    • Takahashi, S.Y.1    Zhao, X.2    Kageyama, T.3    Yamamoto, Y.4
  • 26
    • 0019888345 scopus 로고
    • The structure of vitellogenin
    • Wiley HS, Wallace RA. The structure of vitellogenin. J Biol Chem 1981;256:8626-34.
    • (1981) J Biol Chem , vol.256 , pp. 8626-8634
    • Wiley, H.S.1    Wallace, R.A.2
  • 27
    • 0028023542 scopus 로고
    • Cathepsin D. Activity in the vitellogenesis of Xenopus laevis
    • Yoshizaki N, Yonezawa S, Cathepsin D. Activity in the vitellogenesis of Xenopus laevis. Dev Growth Differ 1994;36:299-306.
    • (1994) Dev Growth Differ , vol.36 , pp. 299-306
    • Yoshizaki, N.1    Yonezawa, S.2
  • 28
    • 0029992556 scopus 로고    scopus 로고
    • Salt concentration-dependency of vitellogenin processing by cathepsin D in Xenopus laevis
    • Yoshizaki N, Yonezawa S. Salt concentration-dependency of vitellogenin processing by cathepsin D in Xenopus laevis. Dev Growth Differ 1996;38:549-56.
    • (1996) Dev Growth Differ , vol.38 , pp. 549-556
    • Yoshizaki, N.1    Yonezawa, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.