Phaseolin subjected to limited proteolysis by papain-like proteinase: Primary structure and crystallization

Rotari Vitalie; Prak Krisna; Stepurina Tatiana; Morari Diana; Lapteva Natalya; Mikami Bunzo; Utsumi Shigeru; Wilson Karl; Shutov Andrei

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994

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2022-07-09 11:42

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ROTARI, Vitalie, PRAK, Krisna, STEPURINA, Tatiana, MORARI, Diana, LAPTEVA, Natalya, MIKAMI, Bunzo, UTSUMI, Shigeru, WILSON, Karl, SHUTOV, Andrei. Phaseolin subjected to limited proteolysis by papain-like proteinase: Primary structure and crystallization. In: Studia Universitatis Moldaviae (Seria Ştiinţe Reale şi ale Naturii), 2008, nr. 2(12), pp. 19-22. ISSN 1814-3237.

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Studia Universitatis Moldaviae (Seria Ştiinţe Reale şi ale Naturii)

Numărul 2(12) / 2008 / ISSN 1814-3237 /ISSNe 1857-498X

Phaseolin subjected to limited proteolysis by papain-like proteinase: Primary structure and crystallization

Pag. 19-22

Rotari Vitalie, Prak Krisna, Stepurina Tatiana, Morari Diana, Lapteva Natalya, Mikami Bunzo, Utsumi Shigeru, Wilson Karl, Shutov Andrei

Moldova State University

Disponibil în IBN: 11 decembrie 2013

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Fazeolina, globulina de rezervă 7S din cotiledoanele seminţelor de Phaseolus vulgaris a fost supusă proteolizei limitate cu proteinaza papainică endogenă PP purificată din cotiledoanele plantulelor de fasole de 6 zile. Digestul a fost separat în două fracţii: prima cu masă moleculară mare (fazeolina-PP care reţine structura cuaternară), iar a doua cu masă moleculară mică (peptide eliberate). Structura primară completă a fazeolinei-PP a fost descrisă în baza rezultatelor combinate a mass-spectrometriei peptidelor eliberate şi a secvenării amino-terminale a fazeolinei-PP. Au fost obţinute câteva tipuri de cristale ale fazeolinei-PP. Cel mai bun cristal cu rezoluţia difracţiei razelor X de 5,5 Å a fost găsit că aparţine grupei spaţiale P6322, care diferă de grupa spaţială a cristalelor fazeolinei intacte. Este discutat rolul posibil al proteolizei limitate a fazeolinei induse de PP la degradarea ei in vivo.

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