Zobrazeno 1 - 6
of 6
pro vyhledávání: '"R C, Bateman"'
Autor:
M, Hall, P A, Sykes, D L, Fairclough, L J, Lucchese, P, Rogers, W, Staruszkiewicz, R C, Bateman
Publikováno v:
Journal of AOAC International. 82(5)
This study describes the production of a solid-phase assay (test strip/dipstick test) for putrescine and cadaverine in tuna based on the coupling of an amine oxidase to a peroxidase/dye system. The assay was linear to 75 microM in phosphate buffer, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::624098b77dbb6f3072d30b33f9ed07e1
https://pubmed.ncbi.nlm.nih.gov/10513011
https://pubmed.ncbi.nlm.nih.gov/10513011
Autor:
J M, McCoy-Messer, R C, Bateman
Publikováno v:
BioTechniques. 15(2)
The commonly used horseradish peroxidase dye substrate, 2,2'-azino-bis(3-ethyl-benzthiazoline-6-sulphonic acid) (ABTS), was found to be unstable under certain conditions after reaction with the peroxidase. A survey of several buffers and pH values sh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::02a217f0b76cc6dfafafd17c37885bb1
https://pubmed.ncbi.nlm.nih.gov/8373594
https://pubmed.ncbi.nlm.nih.gov/8373594
Publikováno v:
The Journal of biological chemistry. 265(15)
Neutral endopeptidase 24.11 is rapidly inactivated by N-bromoacetyl-D-leucylglycine in a reaction which follows first-order kinetics at pH 8 and 37 degrees C. The concentration dependence of inactivation revealed saturation kinetics with an apparent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f991a99f67119f6d7d40e1b37fb4fe84
https://pubmed.ncbi.nlm.nih.gov/2341387
https://pubmed.ncbi.nlm.nih.gov/2341387
Autor:
R C, Bateman, L B, Hersh
Publikováno v:
Drug design and delivery. 2(1)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::76e17099b36c854a2b70d81773239080
https://pubmed.ncbi.nlm.nih.gov/3334545
https://pubmed.ncbi.nlm.nih.gov/3334545
Publikováno v:
The Journal of biological chemistry. 260(16)
An abiotic system is described which chemically catalyzes the formation of less than Glu-His-Pro-NH2 (thyrotropin-releasing hormone) from less than Glu-His-Pro-amino acid in the presence of copper, ascorbate, and molecular oxygen. Evidence is present
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::04f67a8e824124f3f4bb021f021edece
https://pubmed.ncbi.nlm.nih.gov/3926762
https://pubmed.ncbi.nlm.nih.gov/3926762
Publikováno v:
The Journal of biological chemistry. 264(11)
Neutral endopeptidase 24.11 contains an active-site arginine residue involved in binding the free carboxylate of substrate peptides and inhibitors. This arginine reacts rapidly with [14C]phenylglyoxal, and its reaction is selectively blocked by the p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8bbd7df936708e1ee7781271be3d8dfb
https://pubmed.ncbi.nlm.nih.gov/2703483
https://pubmed.ncbi.nlm.nih.gov/2703483