Facultatea de Biologie și Geoştiinţe / Faculty of Biology and Geosciences

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    ANALIZA HIDROLIZEI VICILINEI ŞI FAZEOLINEI DE CĂTRE PAPAINĂ LA pH ACID
    (CEP USM, 2009) Stepurina, Tatiana; Gașina, Natalia; Morari, Diana; Rotari, Vitalie I.
    The vicilin and phaseolin proteolysis by papain at acidic pH has been studied in vitro. It has been found that vetch vicilin is practically completely degradated at pH 4.6. The phaseolin hydrolysis differs from that of vicilin, phaseolin beingonly modifi ed by papain. This modification results in the formation of fragments that correspond to half subunits of native phaseolin that are resistant to further action of papain. These fragments remain associated in molecule’s quaternary structure producing phaseolin-Pap. The phaseolin modified at pH 4.6 becomes insoluble, while at pH 5.6 it is soluble. The sefindings show that while the action of papain on vicilin is similar to the action of endogenouse papin-like proteinases its action on phaseolin is slightly different.
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    PURIFICAREA ŞI CARACTERIZAREA PARŢIALĂ A PROTEINAZEIA DIN SEMINŢELE GERMINATE DE FASOLE
    (CEP USM, 2007) Rotari, Vitalie I
    Proteinase A, that possibly participate in the degradation of phaseolin, the main 7S storage protein of kidney bean (Phaseolus vulgarisL.), was isolated asa35 kDapolypeptide from germinating kidney bean seeds and partially charac-terised. According to its properties it belong to a group of homologous cysteine proteinases of the papain family that participate in storage protein mobilisation during seeds geminating of many plants. The proteinases of this group hydrolize storage proteins to short peptides. Dispite close similarity to proteinase A from vetch, proteinase A from kidney bean hydrolyse phaseolin by non-co-operative m echanism. This action is limited to the cleavage of subunits into two approxi-mately equal parts and to spliting off a number of short peptideswhich result in the modification of quaternary structure of phaseolin molecule. It is similar to the action on phaseolin of other proteases, both endogenous and exogenous, and provide another example of the importance of phaseolin structure in the explanation of its resistance to proteolysis.
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    THE COMPARATIVE ANALYSIS OF IN VITRO PHASEOLIN PROTEOLYSIS BY PAPAIN AT DIFFERENT pH VALUES
    (CEP USM, 2012) Stepurina, Tatiana; Rotari, Vitalie I.
    Hidroliza fazeolinei native, proteina de rezervă principală din seminţele de fasole (Phaseolus vulgaris L.), de către papaină la diferite valori ale pH-ului, în diapazonul 4,6-8,0, a fost studiată în condiţii invitro. A fost determinat căfaseolina este modificată de către proteoliza limitatăa toate pH-urile investigate. Această modificare rezultăîn formarea fragmentelor ce corespund aproximativ jumătăţii de subunitate a fazeolinei native, care rămân asociate în structura cuaternară amoleculei,producând fazeolina-Pap. La pH-uri mai înalte de 6,2 o parte din fazeolina-Pap este complet hidrolizată de către papaină, ceea ce indică la faptul că asocierea fazeolinei în structuri supramoleculare la pH acid îi conferă, probabil, rezistenţă la proteoliză.