Zobrazeno 1 - 10
of 60
pro vyhledávání: '"Horton Hr"'
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 827:140-143
Covalent chromatographically isolated bovine kidney sulfhydryl oxidase was found to catalyze the oxidation of cysteine and cysteine-containing substrates as determined by assaying with 5,5'-dithiobis(2-nitrobenzoate). Monitoring the time-course of su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d954f7bdab729093e91b5794271ad144
https://doi.org/10.1016/0167-4838(85)90082-2
https://doi.org/10.1016/0167-4838(85)90082-2
Publikováno v:
Biochemistry. 12:5278-5285
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b340606a71daf2d8e80fdae927aafa1c
https://doi.org/10.1021/bi00750a009
https://doi.org/10.1021/bi00750a009
Publikováno v:
Experimental Biology and Medicine. 140:1451-1455
SummaryInvestigation of the air-reoxidation of denatured, fully reduced chymotrypsinogen A resulted in a maximum recovery of 1.4% of enzymatically active chymotrypsin upon treatment with trypsin. Under the same conditions, urea-denatured chymotrypsin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::504acaf0b61231b2a654c3fd4de6f793
https://doi.org/10.3181/00379727-140-36694
https://doi.org/10.3181/00379727-140-36694
Autor:
Koshland De, Horton Hr
Publikováno v:
Journal of the American Chemical Society. 87:1126-1132
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1b8ae0c0b1df7a5aa2ee8a733e0a3d73
https://doi.org/10.1021/ja01083a033
https://doi.org/10.1021/ja01083a033
Publikováno v:
Biochemistry. 3:349-355
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79d30f7884196fea572db57b62b913bd
https://doi.org/10.1021/bi00891a009
https://doi.org/10.1021/bi00891a009
Publikováno v:
Biochimica et biophysica acta. 915(2)
The rate of oxidation of glutathione by solubilized sulfhydryl oxidase was significantly enhanced in the presence of horseradish peroxidase (donor:hydrogen-peroxide oxidoreductase, EC 1.11.1.7). This enhancement was proportional to the amount of acti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83deb4583f5dbb546ff8f8a2680bd533
https://pubmed.ncbi.nlm.nih.gov/3115296
https://pubmed.ncbi.nlm.nih.gov/3115296
Autor:
Horton Hr, Swaisgood He
Publisher Summary This chapter discusses the immobilization as a means of investigating the acquisition of tertiary structure in chymotrypsinogen. Immobilization of chymotrypsinogen through covalent attachment to an insoluble matrix provided the key
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::00f47f6528bdae99ad90fd9fb252f65b
https://doi.org/10.1016/s0076-6879(76)44037-5
https://doi.org/10.1016/s0076-6879(76)44037-5
Publikováno v:
Biochemistry. 18(22)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cf3a49f323fb3e5cd50d7c666efd49d
https://pubmed.ncbi.nlm.nih.gov/508722
https://pubmed.ncbi.nlm.nih.gov/508722
Autor:
Horton Hr, Swaisgood He
Publisher Summary Characterization of immobilized species has been restricted to kinetic studies or to examination of fluorescent spectra because of the limitations imposed by the immobilization matrix. Among the approaches that have been used are de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4add90f75f43c1d93d7720798056d29c
https://doi.org/10.1016/0076-6879(87)35070-0
https://doi.org/10.1016/0076-6879(87)35070-0
Publikováno v:
Biochemistry. 13(10)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::394a2acf1668a7a1d7462d0a4ead1623
https://pubmed.ncbi.nlm.nih.gov/4597070
https://pubmed.ncbi.nlm.nih.gov/4597070