000 01526 a2200493 4500
005 20250512125343.0
264 0 _c19731216
008 197312s 0 0 eng d
022 _a0006-2960
024 7 _a10.1021/bi00744a005
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aStroupe, S D
245 0 0 _aFurther studies of the sulfhydryl-catalyzed isomerization of bovine mercaptalbumin.
_h[electronic resource]
260 _bBiochemistry
_cSep 1973
300 _a3824-30 p.
_bdigital
500 _aPublication Type: Journal Article
650 0 4 _aAnimals
650 0 4 _aBinding Sites
650 0 4 _aCattle
650 0 4 _aCharcoal
650 0 4 _aChromatography, Gel
650 0 4 _aCircular Dichroism
650 0 4 _aDialysis
650 0 4 _aDrug Stability
650 0 4 _aElectrophoresis, Polyacrylamide Gel
650 0 4 _aHalf-Life
650 0 4 _aHydrogen-Ion Concentration
650 0 4 _aIsomerism
650 0 4 _aKinetics
650 0 4 _aMathematics
650 0 4 _aOptical Rotatory Dispersion
650 0 4 _aOsmolar Concentration
650 0 4 _aProtein Binding
650 0 4 _aProtein Conformation
650 0 4 _aProtein Denaturation
650 0 4 _aSerum Albumin, Bovine
_xanalysis
650 0 4 _aSpectrophotometry, Ultraviolet
650 0 4 _aSulfhydryl Compounds
_xanalysis
650 0 4 _aTime Factors
650 0 4 _aTrypsin
700 1 _aFoster, J F
773 0 _tBiochemistry
_gvol. 12
_gno. 20
_gp. 3824-30
856 4 0 _uhttps://doi.org/10.1021/bi00744a005
_zAvailable from publisher's website
999 _c4798978
_d4798978