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Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1116:297-304
Procedures for the unambiguous detection and for the isolation and mass spectrometric identification of pyrroloquinoline quinone (PQQ) are presented. The procedure involved acid hydrolysis of protein in the presence of phenylhydrazine and successive
Autor:
S. Cambi, F. Buffoni
Publikováno v:
Analytical Biochemistry. 187:44-50
A method for the isolation and identification of covalently bound pyridoxal phosphate (PLP) contained in some enzymatic proteins is presented. The method involves acid hydrolysis of the protein in the presence of phenylhydrazine, separation of the ad
Publikováno v:
The International journal of periodonticsrestorative dentistry. 21(4)
The dental transplant was already in use more than 2,000 years ago, reaching a peak in the Middle Ages, but it was only after the 1950s that this subject appeared in the scientific literature. This article describes the case of a young woman whose ma
Publikováno v:
International Journal of Molecular Medicine.
A benzylamine oxidase (E.C. 1.4.3.6) has been purified from pig heart. Western blot analysis showed that the enzyme cross-reacts with a polyclonal antibody raised against homogeneous, crystalline pig plasma benzylamine oxidase (BAO). A subunit molecu
Publikováno v:
Journal of neural transmission. Supplementum. 52
A semicarbazide-sensitive amine oxidase (SSAO) (E.C.1.4.3.6) has been purified from pig heart. Western blot analysis showed that the enzyme reacts with a polyclonal antibody raised against homogeneous crystalline pig plasma benzylamine oxidase (BAO).
Publikováno v:
MAO — The Mother of all Amine Oxidases ISBN: 9783211830376
A semicarbazide-sensitive amine oxidase (SSAO) (E.C.1.4.3.6) has been purified from pig heart. Western blot analysis showed that the enzyme reacts with a polyclonal antibody raised against homogeneous crystalline pig plasma benzylamine oxidase (BAO).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::80d0c6efcd000df105e2478fd082c5ee
https://doi.org/10.1007/978-3-7091-6499-0_26
https://doi.org/10.1007/978-3-7091-6499-0_26
Publikováno v:
Comparative biochemistry and physiology. Part B, Biochemistrymolecular biology. 115(2)
Lung, heart tissues and blood plasma of guinea pigs were investigated to see if tissue-bound semicarbazide-sensitive amine oxidase activities with a high affinity for benzylamine (Bz.SSAO) were present in this species as well as in others. This paper
Publikováno v:
Journal of neural transmission. Supplementum. 41
A semicarbazide-sensitive amine oxidase activity with a high affinity for benzylamine (Bz.SSAO) (E.C. 1.4.3.6) is present in guinea pig dorsal skin. This enzymic activity oxidized benzylamine, histamine, 1,4-methylhistamine and acetylputrescine and w