Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)


J Mol Biol 1979 Sep 05
PMID:Mixed gelation theory. Kinetics, equilibrium and gel incorporation in sickle hemoglobin mixtures. 9 43


Mol Immunol 1979 Sep
PMID:The location and expression of idiotypic determinants in the immunoglobulin variable region--III. Expression of the protein 315 and 460 idiotypic determinants in mouse anti-Dnp antibodies. 9 94


Mol Immunol 1979 Sep
PMID:Immunogenicity of rifamycins. 9 95


Mol Immunol 1979 Sep
PMID:Partial amino acid sequences of rabbit and rat beta 2-microglobulins. 9 96


J Mol Biol 1979 Sep 15
PMID:The fate of norleucine as a replacement for methionine in protein synthesis. 9

From previous work (Guiard, B., Groudinsky, O. and Lederer, F. (1974) Proc. Natl. Acad. Sci. U.S. 71, 2539-2543) it is now clear that the overall secondary and tertiary structure of cytochrome b2 core is very similar to that of cytochrome b5. We present here a direct comparison of circular dichroism spectra and low-temperature absorption spectra which bring further evidence about this structural similarity. Cytochrome b2 core reacts only sluggishly with cytochrome b5 reductase, showing a lack of correspondence with the reductase binding area in cytochrome b5. On the other hand, literature data indicate similar electron transfer rates between cytochrome c on one hand, cytochrome b5 and cytochrome b2 core on the other hand. A structural inspection of cytochrome b2 core suggests that the mouth of the heme crevice in the latter is the most likely region for interaction with cytochrome c, with perhaps ionic bonds slightly different from those proposed by Salemme (Salemme, F.R. (1976) J. Mol. Biol. 102, 563--568) for the cytochrome c-cytochrome b5 interaction. In view of this partial surface similarity, the lack of immunological cross-reactivity between the two hemoprotein cores is attributed to their close similarity with the cytochrome b5 of the antibody-producing rabbit.
Biochim Biophys Acta 1978 Sep 26
PMID:Surface differences and similarities in two homologous proteins. Cytochrome b5 and cytochrome b2 core. 10 Dec 51

The contractile sheaths of five defective, PBS X-like bacteriophages from Bacillus subtilis and B. licheniformis were investigated by electron microscopy, dodecylsulphate gel electrophoresis and immunodiffusion. Electron microscope images of the extended and contracted sheaths were of similar appearance, although their lengths were different. The surface lattices of both the extended and the contracted sheaths were determined by optical diffraction. This showed that the quaternary structure of the sheaths of all five defective phages originated from identical surface lattices, which could be approximately expressed by the selection rules L = -2n' + 3m and L = 9N' + 17M for the extended and contracted sheaths respectively, in which 6n' = n with n = 0 or an integer multiple of 6. These results indicated that the packing of the protein subunits in these sheaths differed from those of other bacteriophages, for example T4 and millimicron [Amos and Klug, J. Mol. Biol. 99, 51--73 (1975); Admiraal and Mellema, J. Ultrastruct. Res. 56, 48--64 (1976)]. The molecular weight of the main sheath protein of the defective phages, as determined by dodecylsulphate gel electrophoresis, was approximately 50000. This value differed from that for T4, but was similar to that of millimicron [Admiraal and Mellema, J. Ultrastruct. Res. 56, 48--64 (1976); King and Laemmli, J. Mol. Biol, 75, 315--337 (1973)]. The results of immunodiffusion experiments, however, pointed to a chemical difference between the sheath proteins of the defective phages and millimicron, in addition to T4.
Eur J Biochem 1978 Sep 01
PMID:The quaternary structure of the sheaths of defective phages similar to PBS X. 10 70


J Mol Biol 1978 Sep 05
PMID:Freezing of dCMP aminohydrolase in the activated conformation by glutaraldehyde. 10 72


J Mol Biol 1978 Sep 05
PMID:Molecular structure of crystalline Streptomyces griseus protease A at 2.8 A resolution. I. Crystallization, data collection and structural analysis. 10 73


J Mol Biol 1978 Sep 05
PMID:Molecular structure of crystalline Streptomyces griseus protease A at 2.8 A resolution. II. Molecular conformation, comparison with alpha-chymotrypsin and active-site geometry. 10 74


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