Proteins major urinary protein complex

Finlayson, J.S., Potter, M Runner, C.R. 1963. Electrophoretic variation and sex dimorphism of the Major Urinary Protein complex in inbred mice a new genetic marker. J. Nat. Cancer Inst. 31,91—107... 

Finlayson, J.S., Asofsky, R., Potter, M. Runner, C.C. 1965. Major Urinary Protein complex of normal mice origin. Science, 149, 981—982. 

A major effort in contemporary olfactory research has focused upon determining the genetic basis of odours of individuality in mice with both major urinary proteins (MUPs) and the major histocompatibility complex (MHC) believed to provide a contribution to discriminable individual differences (Singer, Beauchamp and Yamazaki 1997 Hurst and Beynon 2004). Many of these studies utilized instrumental conditioning tasks in which the animals were rewarded for learning to discriminate between odours. While these experiments demonstrate what an animal... 

Fig. 17.9 The H assignment of the unlabeled pheromone 2-see-butyl-4,5-dihydrothiazole, bound to [U-13C, 15N]-labeled mouse major urinary protein I, was accomplished by comparing the 2D TOCSY spectrum of free ligand (A) to the 13C-fil-tered TOCSY spectrum of the complex (B). Reproduced with permission from Ref. [37]. Copyright 1999 American Chemical Society.

Groen, A., and A. J. Lagerwerf. 1979. Genetically determined electrophoretic variants of the major urinary protein (Mup) complex in mouse urine. Animal Blood Groups and Biochemical Genetics 10 107-114. 

A second highly polymorphic system that contributes to the urinary scents of mice is the major urinary protein (MUP) complex (Beynon and Hurst, 2003). These small lipocalin proteins have a central cavity that binds and releases semiochemicals. Unlike MHC, the only known function of these proteins is in chemical signalling and they are... 

The urinary scents of wild house mice provide each individual with a unique olfactory signature. Two highly polymorphic gene clusters appear to provide the main basis for individuality scents in mice the major histocompatibility complex (MHC) and the major urinary proteins (MUPs) (see Thom et al. and Hurst et al., this volume). These... 

NMR relaxation experiments, however, show that the backbone flexi-bihty of mouse major urinary protein-I (MUP-I) increases upon binding the hydrophobic pheromone 2-5ec-butyl-4,5-dihydrothiazole [173]. The associated increase in backbone conformational entropy of the protein appears to make a substantial contribution towards stabilization of the protein-pheromone complex. To predict accurately the affinity of a protein for a given ligand, it is essential to have prior knowledge of both the enthalpy of binding, and the entropy of binding, ASt . To this end, the entro-... 

Radioimmunoassay. Antibodies can be produced against bile acid-protein complexes - usually bile acid-bovine serum albumin complex - and used for radioimmunoassay of that bile acid in usual manner (cf. 1). Each bile acid should have its own antibody so that the method is suitable for the quantitation of individual bile acids provided the antibodies are specific enough. One of the major problems actually is the cross-reactivity of antibodies and difficulties in the determination of total bile acids in biological materials. Thus, for the fec il bile acids with mainly bacterial transformation products (see Fig. 1) and to some extent for the urinary bile acids, especially under diseased conditions, this is quite Impossible. 

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