22-kDa protein

The His-tagged MBP-MS2 coat fusion protein (HMM) used in this method was created to allow the protein to be immobilized on both Ni2+ or amylose affinity resins. HMM is a 59-kDa protein containing an NT-terminal hexahistidine (6x His) tag, a central maltose-binding protein (MBP) domain, and a C-terminal MS2 coat protein containing the V29/dIFG mutations, which prevent protein multimerization and increase its affinity for RNA (Lim and Peabody, 1994). The protein is expressed in E. coli from plasmid pHMM, which confers kanamycin resistance, and purified using affinity chromatography. 

The van Eys s group has recently reported that a 59 kDa protein that maps to chromosome 22 named smoothelin is exclusively expressed in the contractile SMC phenotype in evolutionarily different species [74-76]. The synthetic SMC phenotype expressed at early stages of development in humans [75] and in chicken [74] does not contain this protein (see also Fig. 5). Smoothelin is not expressed in striated muscles or in mixed SMC-NM cell phenotypes such as myofibroblasts, pericytic venules and myoepithelial cells [74,75]. In SMC, smoothelin is not localized in the intermediate filament network but probably with the actin cytoskeletal systems [76]. In the chicken gizzard, smoothelin exists as multiple isoelectric variants of the 59 kDa molecule, whereas in the vascular SM is present as a 95 kDa variant [76]. 

Trifluoroacetylchloride is very reactive, and therefore, if any of it escapes from the vicinity of the cytochromes P-450 in the smooth endoplasmic reticulum, it might be expected to react with those proteins in highest concentration. The 59-kDa polypeptide, a microsomal carboxylesterase, constitutes 1.5% of the total microsomal protein, and therefore it fulfils this... 

Hedbom E, Heinegard D. Interaction of a 59-kDa connective tissue matrix protein with collagen I and collagen II. J Biol Chem 1989 264 6898-6905. Neame PJ, Kay CJ, McQuillan DJ, Beales MP, Hassell JR. Independent modulation of collagen fibrillogenesis by decorin and lumican. Cell Mol Life Sci 2000 57 859-863. 

Cox, M. A.,Jenh, C. H., Gonsiorek, W., Fine, J., Narula, S. K., Zavodny, P.J., etal. (2001). Human interferon-inducible 10-kDa protein and human interferon-inducible T cell alpha chemoattractant are aHotopic ligands for human CXCR3 Differential binding to receptor states. Molecular Pharmacology, 59(4), 707-715. 

Within the MQa and monomeric part of MQc, the heterogeneous density distribution indicates even the presence of subunits. This can be seen much better in the original picture (20). These may be attributed to the 2 big proteins of PS I with apparent masses of 64 and 59 kDa. Together with the side view (not shown) one gets the dimension and orientation of the trimer within the membrane as shown in Fig. 2,right, similar to the result in (7), which were however solubilized in OGP. The height corresponds to the thickness of the membrane. Obviously, larger hydrophilic parts do not extend from the membrane. This is very different from the architecture of purple bacteria (30). 

The Nlcotiana Fi3 is Imported into spinach mitochondria (Fig. 1, lane 2). The 59 kDa precursor is processed to a 51 kDa protein which was insensitive to externally added protease. The Neurospora Fit gives one major translation product of 56 kDa (Fig. 2, lane 1) which was imported and processed to 54 kDa (Fig. 2. lane 2). The import of the Neurospora FiP needs a membrane potential which is shown in Fig. 2. lane 4 and 5. Addition of valinomycin and oligomycin inhibits thO formation of the membrane potential, no imported products are present. 

Fungal laccases (benzenediokoxygen oxidoreductase, EC 1.10.3.2) belong to the multicopper blue phenoloxidases. They comprise glycosylated proteins expressed in multiple forms and variable molecular weight, ranging from 59 to 110 kDa. Laccase is expressed as multiple constitutive and induced isoenzymes [30, 64]. The enzyme contains four copper atoms (Cu), in different states of oxidation (I, II, III) [65], which play an important role in the catalytic mechanism. Laccase oxidizes different compounds while reducing O2 to H20, a total reduction of four electrons. 

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