000			01475 a2200397 4500
005			20250512021842.0
264		0	_c19880421
008			198804s 0 0 eng d
022			_a0014-5793
024	7		_a10.1016/0014-5793(88)81137-2 _2doi
040			_aNLM _beng _cNLM
100	1		_aYagami, T
245	0	0	_aAdenosine di-, tri- and tetraphosphopyridoxals modify the same lysyl residue at the ATP-binding site in adenylate kinase. _h[electronic resource]
260			_bFEBS letters _cMar 1988
300			_a261-4 p. _bdigital
500			_aPublication Type: Journal Article; Research Support, Non-U.S. Gov't
650	0	4	_aAdenine Nucleotides _xpharmacology
650	0	4	_aAdenosine Diphosphate _xanalogs & derivatives
650	0	4	_aAdenosine Triphosphate _xanalogs & derivatives
650	0	4	_aAdenylate Kinase _xantagonists & inhibitors
650	0	4	_aAmino Acids _xanalysis
650	0	4	_aAnimals
650	0	4	_aBinding Sites
650	0	4	_aKinetics
650	0	4	_aMuscles _xenzymology
650	0	4	_aPeptide Fragments _xanalysis
650	0	4	_aPhosphotransferases _xantagonists & inhibitors
650	0	4	_aProtein Binding
650	0	4	_aPyridoxal _xanalogs & derivatives
650	0	4	_aPyridoxal Phosphate _xanalogs & derivatives
650	0	4	_aRabbits
700	1		_aTagaya, M
700	1		_aFukui, T
773	0		_tFEBS letters _gvol. 229 _gno. 2 _gp. 261-4
856	4	0	_uhttps://doi.org/10.1016/0014-5793(88)81137-2 _zAvailable from publisher's website
999			_c2836958 _d2836958