PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2476174-8 1989 Comparison of ESR results obtained from spin-labeling methylamine-treated or protease-reacted alpha 2M with those from spin-labeling of the free SH groups in intermediate-form alpha 2M shows that trapped protease influences the mobility of the attached nitroxide either through direct contact or by producing a different conformation from that present in methylamine-treated or intermediate-form alpha 2M. Hydroxylamine 253-262 alpha-2-macroglobulin Homo sapiens 94-102 2476174-8 1989 Comparison of ESR results obtained from spin-labeling methylamine-treated or protease-reacted alpha 2M with those from spin-labeling of the free SH groups in intermediate-form alpha 2M shows that trapped protease influences the mobility of the attached nitroxide either through direct contact or by producing a different conformation from that present in methylamine-treated or intermediate-form alpha 2M. Hydroxylamine 253-262 alpha-2-macroglobulin Homo sapiens 176-184 2476174-8 1989 Comparison of ESR results obtained from spin-labeling methylamine-treated or protease-reacted alpha 2M with those from spin-labeling of the free SH groups in intermediate-form alpha 2M shows that trapped protease influences the mobility of the attached nitroxide either through direct contact or by producing a different conformation from that present in methylamine-treated or intermediate-form alpha 2M. Hydroxylamine 253-262 alpha-2-macroglobulin Homo sapiens 176-184 2439371-4 1987 Covalent binding is abolished when the reaction of alpha 2M with the protease is carried out in the presence of hydroxylamine. Hydroxylamine 112-125 alpha-2-macroglobulin Homo sapiens 51-59 6193011-2 1983 The thrombin-alpha 2M binding is normally covalent, but the presence of hydroxylamine during the reaction leads to the formation of a non-covalent complex. Hydroxylamine 72-85 alpha-2-macroglobulin Homo sapiens 13-21 7540989-1 1995 The separations between aromatic residues in the bait region and nitroxide spin labels attached to the thiol ester-forming residues (Cys949 and Gln952) in human alpha 2-macroglobulin (alpha 2M) have been determined from paramagnetic broadening effects of the spin labels on bait region 1H NMR signals. Hydroxylamine 65-74 alpha-2-macroglobulin Homo sapiens 161-182 7540989-1 1995 The separations between aromatic residues in the bait region and nitroxide spin labels attached to the thiol ester-forming residues (Cys949 and Gln952) in human alpha 2-macroglobulin (alpha 2M) have been determined from paramagnetic broadening effects of the spin labels on bait region 1H NMR signals. Hydroxylamine 65-74 alpha-2-macroglobulin Homo sapiens 184-192 3026342-14 1986 Reaction of diethyl pyrocarbonate-treated alpha 2M with hydroxylamine reversed derivatization of 43 of the 53 histidine residues. Hydroxylamine 56-69 alpha-2-macroglobulin Homo sapiens 42-50 6197765-0 1983 The alpha 2 macroglobulin/thrombin interaction in the presence of hydroxylamine. Hydroxylamine 66-79 alpha-2-macroglobulin Homo sapiens 4-25 6197765-1 1983 The influence of a primary amine, hydroxylamine, on the interaction between alpha 2 macroglobulin (alpha 2M) and thrombin was analyzed by electrophoretic and enzymatic methods. Hydroxylamine 34-47 alpha-2-macroglobulin Homo sapiens 76-97 6197765-1 1983 The influence of a primary amine, hydroxylamine, on the interaction between alpha 2 macroglobulin (alpha 2M) and thrombin was analyzed by electrophoretic and enzymatic methods. Hydroxylamine 34-47 alpha-2-macroglobulin Homo sapiens 99-107 6197765-2 1983 Hydroxylamine (final concentrations 0.01 M and 0.1 M) was added to the alpha 2M solution 3 to 5 min before thrombin. Hydroxylamine 0-13 alpha-2-macroglobulin Homo sapiens 71-79 33171781-4 2020 METHODS: NMR (Nuclear Magnetic Resonance) and ESR (Electron Spin Resonance) spectroscopy are employed to characterize the paramagnetic perturbation of the extrinsic nitroxide probe Tempol on beta2m in the absence and presence of AuNPs to determine the surface accessibility properties and the occurrence of chemical or conformational exchange, based on measurements conducted under magnetization equilibrium and non-equilibrium conditions. Hydroxylamine 165-174 alpha-2-macroglobulin Homo sapiens 191-197