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Volumn 115, Issue 2, 1997, Pages 827-832

Sodium dodecyl sulfate-stable proteases in chloroplasts

Author keywords

[No Author keywords available]

Indexed keywords

CHLOROPLAST; DODECYL SULFATE SODIUM; ELECTROPHORESIS; PROTEIN PURIFICATION; PROTEINASE;

EID: 0031397433     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.115.2.827     Document Type: Article
Times cited : (26)

References (11)
  • 1
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    • Protein stability and degradation in chloroplasts
    • Adam Z (1996) Protein stability and degradation in chloroplasts. Plant Mol Biol 32: 773-783
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    • Adam, Z.1
  • 2
    • 0029872716 scopus 로고    scopus 로고
    • Degradation of the light-stress protein is mediated by an ATP-independent, serine-type protease under low-light conditions
    • Adamska I, Lindahl M, Roobol-Boza M, Andersson B (1996) Degradation of the light-stress protein is mediated by an ATP-independent, serine-type protease under low-light conditions. Eur J Biochem 236: 591-599
    • (1996) Eur J Biochem , vol.236 , pp. 591-599
    • Adamska, I.1    Lindahl, M.2    Roobol-Boza, M.3    Andersson, B.4
  • 3
    • 0028840312 scopus 로고
    • FtsH, a membrane-bound ATPase, forms a complex in the cytoplasmic membrane of Escherichia coli
    • Akiyama Y, Yoshihisa T, Ito K (1995) FtsH, a membrane-bound ATPase, forms a complex in the cytoplasmic membrane of Escherichia coli. J Biol Chem 270: 23485-23490
    • (1995) J Biol Chem , vol.270 , pp. 23485-23490
    • Akiyama, Y.1    Yoshihisa, T.2    Ito, K.3
  • 4
    • 0000033226 scopus 로고
    • Reorganization of the photosystem II unit in developing thylakoids of higher plants after transfer to darkness. Changes in Chl b, light-harvesting protein content and grana stacking
    • Argyroudi-Akoyunoglou JH, Akoyunoglou A, Kalosakas K, Akoyunoglou G (1982) Reorganization of the photosystem II unit in developing thylakoids of higher plants after transfer to darkness. Changes in Chl b, light-harvesting protein content and grana stacking. Plant Physiol 70: 1242-1248
    • (1982) Plant Physiol , vol.70 , pp. 1242-1248
    • Argyroudi-Akoyunoglou, J.H.1    Akoyunoglou, A.2    Kalosakas, K.3    Akoyunoglou, G.4
  • 5
    • 0027199986 scopus 로고
    • Photoinhibition of photosystem II. Inactivation, protein damage and turnover
    • Aro EM, Virgin I, Andersson B (1993) Photoinhibition of photosystem II. Inactivation, protein damage and turnover. Biochim Biophys Acta 1143: 113-137
    • (1993) Biochim Biophys Acta , vol.1143 , pp. 113-137
    • Aro, E.M.1    Virgin, I.2    Andersson, B.3
  • 6
    • 0002761891 scopus 로고
    • In vitro synthesis and uptake of cytoplasmatically synthesized chloroplast proteins
    • M Edelmann, RB Hallick, N-H Chua, eds, EIsevier Biochemical Press, Amsterdam
    • Bartlett SG, Grossmann AR, Chua N-H (1982) In vitro synthesis and uptake of cytoplasmatically synthesized chloroplast proteins. In M Edelmann, RB Hallick, N-H Chua, eds, Methods in Chloroplast Molecular Biology, Vol 86. EIsevier Biochemical Press, Amsterdam, pp 1081-1091
    • (1982) Methods in Chloroplast Molecular Biology , vol.86 , pp. 1081-1091
    • Bartlett, S.G.1    Grossmann, A.R.2    Chua, N.-H.3
  • 8
    • 0001352689 scopus 로고
    • Evidence for the existence of peptide hydrolase activity associated with chloroplasts isolated from barley mesophyll protoplasts
    • Dalling MG, Tang AB, Huffaker RC (1983) Evidence for the existence of peptide hydrolase activity associated with chloroplasts isolated from barley mesophyll protoplasts. Z Pflanzenphysiol 111: 311-318
    • (1983) Z Pflanzenphysiol , vol.111 , pp. 311-318
    • Dalling, M.G.1    Tang, A.B.2    Huffaker, R.C.3
  • 9
    • 0024275423 scopus 로고
    • Characterization and subcellular localization of aminopeptidases in senescing barley leaves
    • Thayer SS, Choe HT, Rausser S, Huffaker RC (1988) Characterization and subcellular localization of aminopeptidases in senescing barley leaves. Plant Physiol 87: 894-897
    • (1988) Plant Physiol , vol.87 , pp. 894-897
    • Thayer, S.S.1    Choe, H.T.2    Rausser, S.3    Huffaker, R.C.4
  • 10
    • 0027535381 scopus 로고
    • The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression
    • Tomoyasu T, Yuki T, Morimura S, Mori H, Yamanaka K, Niki M, Hiraga S, Ogura T (1993) The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression. J Bacteriol 175: 1344-1355
    • (1993) J Bacteriol , vol.175 , pp. 1344-1355
    • Tomoyasu, T.1    Yuki, T.2    Morimura, S.3    Mori, H.4    Yamanaka, K.5    Niki, M.6    Hiraga, S.7    Ogura, T.8
  • 11
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    • A chloroplast processing enzyme involved in precursor maturation shares a zinc-binding motif with a recently recognized family of metalloendopeptidases
    • VanderVere PS, Bennett TM, Oblong JE, Lamppa GK (1995) A chloroplast processing enzyme involved in precursor maturation shares a zinc-binding motif with a recently recognized family of metalloendopeptidases. Proc Natl Acad Sci USA 92: 7177-7181
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7177-7181
    • Vandervere, P.S.1    Bennett, T.M.2    Oblong, J.E.3    Lamppa, G.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.