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The mouse immunoglobulin A myeloma proteins MOPC 315, MOPC 460 and XRPC 25 all possess dinitrophenyl (Dnp)-binding activity. Differences in specificities were shown by measuring the affinities of a variety of haptens. By using a series of Dnp-spin-labelled haptens, the dimensions of the binding sites of the three myeloma proteins were compared by the method described for protein MOPC 315 [Sutton, Gettins, Givol, Marsh, Wain-Hobson, Willan & Dwek (1977) Biochem. J.165, 177-197]. The dinitrophenyl ring is rigidly held in all three sites. The depths of the sites are all 1.1-1.2nm, but there are differences in the lateral dimensions at the entrance to the sites. For protein XRPC 25 these dimensions are 0.75nmx0.8nm, which may be compared with 0.85nmx1.1nm for protein MOPC 315 and >/=1.0nmx1.1nm for protein MOPC 460. The site in protein MOPC 460 is more symmetrical with respect to the plane of the dinitrophenyl ring than in either of the other two myeloma proteins and also allows greater penetration of solvent. In protein XRPC 25 a positively charged residue was located at the entrance to the site, similarly positioned to that reported for protein MOPC 315 [Sutton, Gettins, Givol, Marsh, Wain-Hobson, Willan & Dwek (1977) Biochem.J.165, 177-197]. All three proteins possess lanthanide-binding sites, but only in protein MOPC 315 is there antagonism between lanthanide and hapten binding. However, the effects of the diamagnetic La(III) on the electron-spin-resonance spectra of bound Dnp spin labels in both proteins MOPC 460 and XRPC 25 suggest an interaction between the two sites. Comparison of this effect with that caused by the addition of the paramagnetic Gd(III) enables the distance between the lanthanide- and hapten-binding sites to be calculated. In both proteins MOPC 460 and MOPC 315 the metal site is approx. 1.0nm from the nitroxide moiety of the spin-labelled hapten, but in protein XRPC 25 this distance is at least 2.0nm.
K J Willan, and
D Marsh, and
C A Sunderland, and
B J Sutton, and
S Wain-Hobson, and
R A Dwek, and
D Givol
August 1977,
The Biochemical journal,
K J Willan, and
D Marsh, and
C A Sunderland, and
B J Sutton, and
S Wain-Hobson, and
R A Dwek, and
D Givol
January 1974,
Biochemistry,
K J Willan, and
D Marsh, and
C A Sunderland, and
B J Sutton, and
S Wain-Hobson, and
R A Dwek, and
D Givol
November 1978,
The Biochemical journal,
K J Willan, and
D Marsh, and
C A Sunderland, and
B J Sutton, and
S Wain-Hobson, and
R A Dwek, and
D Givol
June 1976,
Biochemistry,
K J Willan, and
D Marsh, and
C A Sunderland, and
B J Sutton, and
S Wain-Hobson, and
R A Dwek, and
D Givol
November 1971,
Biochemistry,
K J Willan, and
D Marsh, and
C A Sunderland, and
B J Sutton, and
S Wain-Hobson, and
R A Dwek, and
D Givol
January 1974,
Immunological communications,
K J Willan, and
D Marsh, and
C A Sunderland, and
B J Sutton, and
S Wain-Hobson, and
R A Dwek, and
D Givol
April 1976,
Biochemistry,
K J Willan, and
D Marsh, and
C A Sunderland, and
B J Sutton, and
S Wain-Hobson, and
R A Dwek, and
D Givol
October 1969,
Journal of immunology (Baltimore, Md. : 1950),
K J Willan, and
D Marsh, and
C A Sunderland, and
B J Sutton, and
S Wain-Hobson, and
R A Dwek, and
D Givol
August 1972,
Biochemistry,
K J Willan, and
D Marsh, and
C A Sunderland, and
B J Sutton, and
S Wain-Hobson, and
R A Dwek, and
D Givol
October 1978,
Biochemistry,
