http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Conformational Lock and Dissociative Thermal Inactivation of Lentil Seedling Amine Oxidase
( S. Zahra Moosavi Nejad ),( Ali Akbar Moosavi Movahedi ),( Mostafa Rezaei Tavirani ),( Giovanni Floris ),( Rosaria Medda ) 생화학분자생물학회 2003 BMB Reports Vol.36 No.2
The kinetics of thermal inactivation of copper-containing amine oxidase from lentil seedlings were studied in a 100 mM potassium phosphate buffer, pH 7, using putrescine as the substrate. The temperature range was between 47-60℃. The thermal inactivation curves were not linear at 52 and 57℃; three linear phases were shown. The first phase gave some information about the number of dimeric forms of the enzyme that were induced by the higher temperatures using the conformational lock pertaining theory to oligomeric enzyme. The conformational lock caused two additional dimeric forms of the enzyme when the temperature increased to 50℃. The second and third phases were interpreted according to a dissociative thermal inactivation model. These phases showed that lentil amine oxidase was reversibly-dissociated before the irreversible thermal inactivation. Although lentil amine oxidase is not a thermostable enzyme, its dimeric structure can form conformational lock, conferring a structural tolerance to the enzyme against heat stress.
Conformational Lock and Dissociative Thermal Inactivation of Lentil Seedling Amine Oxidase
Moosavi-Nejad, S. Zahra,Moosavi-Movahedi, Ali-Akbar,Rezaei-Tavirani, Mostafa,Floris, Giovanni,Medda, Rosaria Korean Society for Biochemistry and Molecular Biol 2003 Journal of biochemistry and molecular biology Vol.36 No.2
The kinetics of thermal inactivation of copper-containing amine oxidase from lentil seedlings were studied in a 100 mM potassium phosphate buffer, pH 7, using putrescine as the substrate. The temperature range was between $47-60^{\circ}C$. The thermal inactivation curves were not linear at 52 and $57^{\circ}C$; three linear phases were shown. The first phase gave some information about the number of dimeric forms of the enzyme that were induced by the higher temperatures using the "conformational lock" pertaining theory to oligomeric enzyme. The "conformational lock" caused two additional dimeric forms of the enzyme when the temperature increased to $57^{\circ}C$. The second and third phases were interpreted according to a dissociative thermal inactivation model. These phases showed that lentil amine oxidase was reversibly-dissociated before the irreversible thermal inactivation. Although lentil amine oxidase is not a thermostable enzyme, its dimeric structure can form "conformational lock," conferring a structural tolerance to the enzyme against heat stress.
Sardinian honeys as sources of xanthine oxidase and tyrosinase inhibitors
Di Petrillo, Amalia,Santos-Buelga, Celestino,Era, Benedetta,Gonzalez-Paramas, Ana Maria,Tuberoso, Carlo Ignazio Giovanni,Medda, Rosaria,Pintus, Francesca,Fais, Antonella 한국식품과학회 2018 Food Science and Biotechnology Vol.27 No.1
Sardinian honeys obtained from different floral sources (Arbutus, Asphodelus, Eucalyptus, Thistle, and Sulla) were evaluated for their ability to inhibit tyrosinase and xanthine oxidase enzymes and for their antioxidant activity. Physicochemical parameters, total phenolic, and flavonoids content were also determined. Honey from Arbutus flowers had the highest antioxidant activity followed by Eucalyptus and Thistle ones. These three honeys showed good tyrosinase and xanthine oxidase inhibition properties. Thus, these Sardinian honeys could have a great potential as antioxidant sources for pharmaceutical and cosmetic applications.