000			01773 a2200493 4500
005			20250513184529.0
264		0	_c19990715
008			199907s 0 0 eng d
022			_a0003-9861
024	7		_a10.1006/abbi.1999.1256 _2doi
040			_aNLM _beng _cNLM
100	1		_aPete, M J
245	0	0	_aA recombinant form of the catalytic subunit of phosphorylase kinase that is soluble, monomeric, and includes key C-terminal residues. _h[electronic resource]
260			_bArchives of biochemistry and biophysics _cJul 1999
300			_a104-14 p. _bdigital
500			_aPublication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
650	0	4	_aAdenosine Triphosphate _xmetabolism
650	0	4	_aAnimals
650	0	4	_aBinding Sites
650	0	4	_aCalmodulin _xmetabolism
650	0	4	_aCalpain _xmetabolism
650	0	4	_aCatalytic Domain _xgenetics
650	0	4	_aChromatography, Liquid
650	0	4	_aEnzyme Stability
650	0	4	_aEscherichia coli _xgenetics
650	0	4	_aKinetics
650	0	4	_aMolecular Weight
650	0	4	_aMuscles _xenzymology
650	0	4	_aPeptide Fragments _xchemistry
650	0	4	_aPhosphorylase Kinase _xchemistry
650	0	4	_aPhosphorylase b _xmetabolism
650	0	4	_aPhosphorylation
650	0	4	_aRabbits
650	0	4	_aRecombinant Proteins _xbiosynthesis
650	0	4	_aSolubility
650	0	4	_aSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
650	0	4	_aStructure-Activity Relationship
650	0	4	_aTemperature
700	1		_aLiao, C X
700	1		_aBartleson, C
700	1		_aGraves, D J
773	0		_tArchives of biochemistry and biophysics _gvol. 367 _gno. 1 _gp. 104-14
856	4	0	_uhttps://doi.org/10.1006/abbi.1999.1256 _zAvailable from publisher's website
999			_c10333869 _d10333869