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Volumn 79, Issue 8, 2014, Pages 820-825

11S storage globulin from pumpkin seeds: Regularities of proteolysis by papain

Author keywords

Cucurbita maxima; kinetics; limited proteolysis; papain; seed storage globulin

Indexed keywords

GLOBULIN; PAPAIN; VEGETABLE PROTEIN;

EID: 84906270938     PISSN: 00062979     EISSN: 16083040     Source Type: Journal    
DOI: 10.1134/S0006297914080100     Document Type: Article
Times cited : (4)

References (15)
  • 1
    • 0002533094 scopus 로고    scopus 로고
    • Distribution and some properties of seed globulins
    • R Shewry R. Casey (eds) Kluwer Academic Publishers Dordrecht 10.1007/978-94-011-4431-5-8
    • Casey, R. (1999) Distribution and some properties of seed globulins, in Seed Proteins (Shewry, P. R.; and Casey, R.; eds.) Kluwer Academic Publishers, Dordrecht, pp. 159-169.
    • (1999) Seed Proteins , pp. 159-169
    • Casey, R.1
  • 3
    • 84906248541 scopus 로고    scopus 로고
    • Seed storage globulins: Their descent from bacterial ancestors and mechanisms of degradation
    • S. D Milford (eds) Nova Science Publishers New York
    • Shutov, A. D.; and Wilson, K. A. (2014) Seed storage globulins: their descent from bacterial ancestors and mechanisms of degradation, in Globulins: Biochemistry, Production and Role in Immunity (Milford, S. D.; ed.) Nova Science Publishers, New York, pp. 71-104.
    • (2014) Globulins: Biochemistry, Production and Role in Immunity , pp. 71-104
    • Shutov, A.D.1    Wilson, K.A.2
  • 4
    • 0035847055 scopus 로고    scopus 로고
    • Crystal structure of soybean proglycinin A1aB1b homotrimer
    • 1:CAS:528:DC%2BD3cXovFyjtrs%3D 11124907 10.1006/jmbi.2000.4310
    • Adachi, M.; Takenaka, Y.; Gidamis, A. B.; Mikami, B.; and Utsumi, S. (2001) Crystal structure of soybean proglycinin A1aB1b homotrimer, J. Mol. Biol.; 305, 291-305.
    • (2001) J. Mol. Biol. , vol.305 , pp. 291-305
    • Adachi, M.1    Takenaka, Y.2    Gidamis, A.B.3    Mikami, B.4    Utsumi, S.5
  • 5
    • 84864917454 scopus 로고    scopus 로고
    • Limited proteolysis regulates massive degradation of glycinin, storage 11S globulin from soybean seeds: An in vitro model
    • 1:CAS:528:DC%2BC38XhtVektbzE 22795747 10.1016/j.jplph.2012.06.004
    • Shutov, A.; Rudakova, A.; Rudakov, S.; Kakhovskaya, I.; Schallau, A.; Maruyama, N.; and Wilson, K. (2012) Limited proteolysis regulates massive degradation of glycinin, storage 11S globulin from soybean seeds: an in vitro model, J. Plant Physiol.; 169, 1227-1233.
    • (2012) J. Plant Physiol. , vol.169 , pp. 1227-1233
    • Shutov, A.1    Rudakova, A.2    Rudakov, S.3    Kakhovskaya, I.4    Schallau, A.5    Maruyama, N.6    Wilson, K.7
  • 6
    • 0013457640 scopus 로고
    • Susceptibility to attack by proteolytic enzymes
    • 1:CAS:528:DyaF1MXksVahsQ%3D%3D 10.1016/S0076-6879(67)11094-X
    • Rupley, J. A. (1967) Susceptibility to attack by proteolytic enzymes, Methods Enzymol.; 11, 905-917.
    • (1967) Methods Enzymol. , vol.11 , pp. 905-917
    • Rupley, J.A.1
  • 7
    • 0142060071 scopus 로고    scopus 로고
    • Applying the increase in rate constants of cooperative proteolysis to the determination of transition curves of protein denaturation
    • 1:CAS:528:DC%2BD3sXnsVagsL0%3D 10.1016/S0165-022X(03)00106-4
    • Vaintraub, I. A.; and Morari, D. (2003) Applying the increase in rate constants of cooperative proteolysis to the determination of transition curves of protein denaturation, Biochem. Biophys. Methods, 57, 191-201.
    • (2003) Biochem. Biophys. Methods , vol.57 , pp. 191-201
    • Vaintraub, I.A.1    Morari, D.2
  • 8
    • 84886713322 scopus 로고    scopus 로고
    • Degradation of β-conglycinin β-homotrimer by papain: Independent occurrence of limited and extensive proteolyses
    • 1:CAS:528:DC%2BC3sXhslGhtbrJ 24096671 10.1271/bbb.130440
    • Shutov, A. D.; Rudakova, A. S.; Rudakov, S. V.; Kakhovskaya, I. A.; Schallau, A. A.; Wilson, K. A.; and Maruyama, N. (2013) Degradation of β-conglycinin β-homotrimer by papain: independent occurrence of limited and extensive proteolyses, Biosci. Biotechnol. Biochem.; 77, 2082-2086.
    • (2013) Biosci. Biotechnol. Biochem. , vol.77 , pp. 2082-2086
    • Shutov, A.D.1    Rudakova, A.S.2    Rudakov, S.V.3    Kakhovskaya, I.A.4    Schallau, A.A.5    Wilson, K.A.6    Maruyama, N.7
  • 9
    • 5144228267 scopus 로고    scopus 로고
    • Comparative study of the role of the major proteinases of germinated common bean (Phaseolus vulgaris L.) and soybean (Glycine max (L.) Merrill) seeds in the degradation of their storage proteins
    • 1:CAS:528:DC%2BD2cXnvVOkt78%3D 15333645 10.1093/jxb/erh247
    • Zakharov, A.; Carchilan, M.; Stepurina, T.; Rotari, V.; Wilson, K.; and Vaintraub, I. (2004) Comparative study of the role of the major proteinases of germinated common bean (Phaseolus vulgaris L.) and soybean (Glycine max (L.) Merrill) seeds in the degradation of their storage proteins, J. Exp. Bot.; 55, 2241-2249.
    • (2004) J. Exp. Bot. , vol.55 , pp. 2241-2249
    • Zakharov, A.1    Carchilan, M.2    Stepurina, T.3    Rotari, V.4    Wilson, K.5    Vaintraub, I.6
  • 10
    • 84859820774 scopus 로고    scopus 로고
    • Mobilization of seed protein reserves
    • 1:CAS:528:DC%2BC38XntV2gur8%3D 22017287 10.1111/j.1399-3054.2011.01535.x
    • Tan-Wilson, A. L.; and Wilson, K. A. (2012) Mobilization of seed protein reserves, Physiol. Plant.; 145, 140-153.
    • (2012) Physiol. Plant. , vol.145 , pp. 140-153
    • Tan-Wilson, A.L.1    Wilson, K.A.2
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 1:CAS:528:DC%2BD3MXlsFags7s%3D 5432063 10.1038/227680a0
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 12
    • 0001194371 scopus 로고
    • Proteolysis of Kunitz soybean inhibitor. Influence on its activity
    • 1:CAS:528:DyaK2MXkvVWlt7w%3D 10.1021/jf00052a003
    • Vaintraub, I. A.; and Yattara, H. B. (1995) Proteolysis of Kunitz soybean inhibitor. Influence on its activity, J. Agric. Food Chem.; 43, 862-868.
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 862-868
    • Vaintraub, I.A.1    Yattara, H.B.2
  • 13
    • 0025861347 scopus 로고
    • Action of trypsin on soybean glycinin. Mixed-type proteolysis and its kinetics; Molecular mass of glycinin-T
    • 1:CAS:528:DyaK3MXkvVyitbc%3D 1868843 10.1111/j.1432-1033.1991.tb16152.x
    • Shutov, A. D.; Pineda, J.; Senyuk, V. I.; Reva, V. A.; and Vaintraub, I. A. (1991) Action of trypsin on soybean glycinin. Mixed-type proteolysis and its kinetics; molecular mass of glycinin-T, Eur. J. Biochem.; 199, 539-543.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 539-543
    • Shutov, A.D.1    Pineda, J.2    Senyuk, V.I.3    Reva, V.A.4    Vaintraub, I.A.5
  • 14
    • 0142073622 scopus 로고    scopus 로고
    • Kinetics of cooperative proteolysis
    • 1:CAS:528:DyaK1cXjsFanu7w%3D 10.1002/(SICI)1521-3803(199804)42:02<59: AID-FOOD59>3.3.CO;2-N
    • Vaintraub, I. A. (1998) Kinetics of cooperative proteolysis, Nahrung, 42, 59-60.
    • (1998) Nahrung , vol.42 , pp. 59-60
    • Vaintraub, I.A.1
  • 15
    • 0037898127 scopus 로고    scopus 로고
    • Storage and mobilization as antagonistic functional constraints of seed storage globulin evolution
    • 1:CAS:528:DC%2BD3sXkvVSms7g%3D 12754262 10.1093/jxb/erg165
    • Shutov, A. D.; Blattner, F. R.; Baumlein, H.; and Muntz, K. (2003) Storage and mobilization as antagonistic functional constraints of seed storage globulin evolution, J. Exp. Bot.; 54, 1645-1654.
    • (2003) J. Exp. Bot. , vol.54 , pp. 1645-1654
    • Shutov, A.D.1    Blattner, F.R.2    Baumlein, H.3    Muntz, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.