Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Constance D. Anderson"'
Publikováno v:
Archives of biochemistry and biophysics. 344(1)
Haemophilus parasuis malate dehydrogenase (( S )-malate:NAD + oxidoreductase; EC 1.1.1.37) isolated from cell sonicates was purified 584-fold to electrophoretic homogeneity with a 19% recovery and a specific activity of 222 units/mg protein. SDS–po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::febeda6fbd96b532f6be7183fe69d276
https://pubmed.ncbi.nlm.nih.gov/9244395
https://pubmed.ncbi.nlm.nih.gov/9244395
Publikováno v:
Biochimica et biophysica acta. 1340(2)
Glucose 6-phosphate oxidation, catalyzed by purified Azotobacter vinelandii glucose 6-phosphate dehydrogenase, was studied with respect to the selective utilization of NAD, NADP, thionicotinamide adenine dinucleotide or thionicotinamide adenine dinuc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::490835cf4811861149e06a81319f4077
https://pubmed.ncbi.nlm.nih.gov/9252113
https://pubmed.ncbi.nlm.nih.gov/9252113
Publikováno v:
Analytical biochemistry. 195(1)
The vinylogue of NAD, 3-pyridylacryloamide adenine dinucleotide, was prepared from NAD and 3-pyridylacryloamide through the snake venom NADase-catalyzed transglycosidation reaction. The analog, purified by ion-exchange chromatography, was obtained in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6eb798ed7fdb96b574a71154ff88477
https://pubmed.ncbi.nlm.nih.gov/1888017
https://pubmed.ncbi.nlm.nih.gov/1888017
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 787:215-220
Nicotinoylacrylic acid and the corresponding methyl, ethyl, propyl and benzyl esters were studied with respect to selective inactivation of dehydrogenases through covalent modification of essential sulfhydryl groups. An effective inactivation of yeas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::50bbe5569d2613c6e8b916f4b8400054
https://doi.org/10.1016/0167-4838(84)90311-x
https://doi.org/10.1016/0167-4838(84)90311-x
Publikováno v:
Analytical Biochemistry. 161:258-261
Human lactate dehydrogenase isozymes, LDH-1 and LDH-5, were inactivated at 25 degrees C and pH 7.5 by N-alkylmaleimides of varying chain length, and by fluorescein mercuric acetate. Second-order rate constants for the inactivation of LDH-5 by N-alkyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d55560128fd297ddc327df560ac6c7e1
https://doi.org/10.1016/0003-2697(87)90449-0
https://doi.org/10.1016/0003-2697(87)90449-0
Publikováno v:
Analytical Biochemistry. 134:50-55
3-Aminopyridine 1,N6-ethenoadenine dinucleotide phosphate (epsilon-AADP) was synthesized from 3-aminopyridine adenine dinucleotide phosphate by reaction with chloroacetaldehyde. The reaction was monitored by high-pressure liquid chromatography. The p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::892c27494c1cffa4baa6f1424c1c9cb5
https://doi.org/10.1016/0003-2697(83)90262-2
https://doi.org/10.1016/0003-2697(83)90262-2
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 997:236-241
A series of N-alkylmaleimides varying in chainlength from N-methyl- to N-octylmaleimide inclusive was shown to effectively inactivate sheep liver sorbitol dehydrogenase at pH 7.5 and 25 degrees C. The apparent second-order rate constants for inactiva
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4911c7bb6334a38359dc259b37726712
https://doi.org/10.1016/0167-4838(89)90193-3
https://doi.org/10.1016/0167-4838(89)90193-3
Autor:
Philip L. Hall, Constance D. Anderson
Publikováno v:
Analytical Biochemistry. 60:417-423
The sulfhydryl proteinase ficin (EC 3.4.4.12) was purified by chromatography on an agarose-mercurial column. Two separate protein fractions were eluted, ficin and mercurificin, both exhibiting enzymatic activity upon activation by excess thiol.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1ccd1afa3e645ec683019471154a183
https://doi.org/10.1016/0003-2697(74)90250-4
https://doi.org/10.1016/0003-2697(74)90250-4
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 994:75-80
Haemophilus influenzae 6-phosphogluconate dehydrogenase (6-phospho- d -gluconate:NADP + 2-oxidoreductase (decar☐ylating), EC 1.1.1.44) was purified 308-fold to electrophoretic homogeneity with a 16% recovery through a five-step procedure involving
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b4645f257a346ae6d2c7a39d86fbd91
https://doi.org/10.1016/0167-4838(89)90064-2
https://doi.org/10.1016/0167-4838(89)90064-2
Publikováno v:
Microbiology. 131:2041-2045
Summary: The 2':3'-cyclic nucleotide phosphodiesterase:3'-nucleotidase of Haemophilus influenzae was purified from a periplasmic preparation by affinity chromatographic techniques. The enzyme-catalysed hydrolysis of 2': 3'-cyclic AMP to adenosine wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edd93509384c9ec3d535e22dd65a399a
https://doi.org/10.1099/00221287-131-8-2041
https://doi.org/10.1099/00221287-131-8-2041