Zobrazeno 1 - 8
of 8
pro vyhledávání: '"G. N. Pruidze"'
Publikováno v:
Food Research International. 36:587-595
Molecular weights, (MW) pH optimum and substrate specificity of multiple forms of phenol oxidases from Kolkhida tea leaves ( Camelia sinensis L.) and microscopic fungus Mycelia sterilia IBR 35219/2 have been studied. It has been shown that Kolkhida t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::900c7659f1021141da924963396c3917
https://doi.org/10.1016/s0963-9969(03)00006-1
https://doi.org/10.1016/s0963-9969(03)00006-1
Publikováno v:
Applied Biochemistry and Microbiology. 36:115-118
Phenol oxidase (EC 1.14.18.1) from the microscopic fungusMycelia sterilia IBR 35219/2 was immobilized using glutaraldehyde on macroporous silica carriers. The enzyme immobilized on amino-Silochrome SKh-2 or aminopropyl-Silochrome 350/80 exhibited max
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::de1203afc2e20cc77d413b17b1609ce6
https://doi.org/10.1007/bf02737904
https://doi.org/10.1007/bf02737904
Publikováno v:
Ukrains'kyi biokhimichnyi zhurnal (1999 ). 72(3)
The intracellular localization and some properties of monophenol monooxygenase (MPMO) from fresh tea leaves have been studied. It has been demonstrated that MPMO activity is located in cytosole and chloroplasts. These two forms have different propert
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::edaf6b063ad7469e394ce2eb2a5904d9
https://pubmed.ncbi.nlm.nih.gov/11200473
https://pubmed.ncbi.nlm.nih.gov/11200473
Publikováno v:
Prikladnaia biokhimiia i mikrobiologiia. 36(2)
Phenol oxidase (EC 1.14.18.1) from the microscopic fungus Mycelia sterilia IBR 35219/2 was immobilized using glutaraldehyde on macroporous silica carriers. The enzyme immobilized on amino-Silochrome SKh-2 or aminopropyl-Silochrome 350/80 exhibited ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::593d272b11ea45e6428e22cc7409ad36
https://pubmed.ncbi.nlm.nih.gov/10779999
https://pubmed.ncbi.nlm.nih.gov/10779999
Publikováno v:
Biokhimiia (Moscow, Russia). 41(10)
Purification of fractions of tea leaves peroxidase is described. During ion-exchange chromatography on DEAE- and CM-cellulose peroxidase is eluted into six fractions, differing in their electrophoretic properties. The enzyme showed optimal activity a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::865f80fd90df8ae20070b11be171c499
https://pubmed.ncbi.nlm.nih.gov/15639
https://pubmed.ncbi.nlm.nih.gov/15639
Autor:
G. N. Pruidze
Publikováno v:
Enzyme Engineering ISBN: 9781468437218
Phenol oxidase (o-diphenol: O2 oxidoreductase, E.C.I.10.3.1.) belongs to the coppercontaining class of enzymes. It is widely distributed in plants, and plays an important role in cell metabolism. The enzyme catalyzes the oxidation of monophenols, pol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f27ada9cc3a4d4fee58343317ce28655
https://doi.org/10.1007/978-1-4684-3719-5_17
https://doi.org/10.1007/978-1-4684-3719-5_17
Publikováno v:
Biokhimiia (Moscow, Russia). 48(7)
The substrate specificity and some kinetic properties of the monomeric (Mr = 26 000--35 000) and dimeric (Mr = 55 000--70 000) forms of phenol oxidase from vine leaves were studied. These forms possess different hydroxylating and o-diphenol oxidase a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::55a5de8ad30b7c4a701ea9937b398756
https://pubmed.ncbi.nlm.nih.gov/6412775
https://pubmed.ncbi.nlm.nih.gov/6412775
Autor:
M A, Bokuchava, G N, Pruidze
Publikováno v:
Izvestiia Akademii nauk SSSR. Seriia biologicheskaia. 1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8a3922e6b0087ebc94ffcef8cabf1dce
https://pubmed.ncbi.nlm.nih.gov/5490986
https://pubmed.ncbi.nlm.nih.gov/5490986