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Query: UMLS:C0271276 (Hudson)
 1,066 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Previous studies [G. S. Hudson et al. (1989) J. Biol. Chem. 265, 808-814] showed that the faster turnover rates and lower affinities for CO2 of ribulosebisphosphate carboxylase/oxygenases from C4 plants, compared to C3 and C3/C4 plants, were specified by the chloroplast-encoded large subunits. In pairs of closely related C3 and C4 species from three genera, these kinetic changes were accompanied by only three to six amino acid residue substitutions, depending on the genus. None of these substitutions occurred near the active site and only one, 309Met (C3) to Ile (C4), was common to all three genera. Unlike the plant carboxylases, the highly homologous enzyme from the cyanobacterium Synechococcus PCC 6301 folds and assembles properly when its rbcL and rbcS genes are coexpressed in Escherichia coli. Furthermore, the cyanobacterial enzyme has Ile at position 309 of the large subunit, a high turnover number, and a poor affinity for CO2. 309Ile was replaced with Met and several other residues by site-directed mutagenesis of the cyanobacterial rbcL. Met and Leu were tolerated at this position with no alteration in the kinetic or structural properties of the assembled holoenzyme. However, substitution with Val, Gly, Trp, or Arg prevented the assembly of the subunits. The indifference to Met or Ile at this position, as well as the tolerance for Leu which is not observed with any natural ribulosebisphosphate carboxylase, leads to the conclusion that either the 309Met/Ile substitution has no effect on the kinetic properties of the plant enzyme, despite the correlation apparent in previous studies, or the cyanobacterial enzyme is sufficiently different from the plant enzyme in other respects that the influence of residue 309 is masked.
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PMID:Effects of mutations at residue 309 of the large subunit of ribulosebisphosphate carboxylase from Synechococcus PCC 6301. 144 69

During the last 15 years pulse oximetry has become a widely accepted method of monitoring during general and local anaesthesia. Pulse oximeters measuring with two wave-lengths are considerably affected by dyshaemoglobin. At concentrations up to 30%, CO-Hb cannot be distinguished from O2-Hb. Met-Hb, even in low concentrations, leads to a constant error of measurement; some authors recommended exploiting this for estimation of the Met-Hb concentration. To prove the aim of the present study was to test whether this error in measurement can be defined with one formula for different pulse oximeters. PATIENTS AND METHODS. In a prospective, randomized, double-blind study, 171 non-smoking patients with healthy lungs (ASA 1-3) who had received a plexus block for hand surgery were investigated. After premedication with 3.75-15 mg medazolam p.o. each patient received a total of 6 1O2 via a Hudson mask during the investigation. After 10 min the following pulse oximeters were put on the index finger: (1) Ohmeda BIOX 3700e, (2) Critikon Oxyshuttle, (3) Nellcor N 180. Simultaneously a venous blood sample was taken and analysed immediately with a Radiometer OSM3. The procedure was repeated 15, 30, 60 and 120 min after the plexus block. In 41 patients the plexus block was carried out with lidocaine (6 mg/kg body weight) and in 130 patients, with prilocaine (7 mg/kg body weight). RESULTS. There were no significant differences in age, sex and risk groups between the lidocaine and the prilocaine group. In the lidocaine group we were able to show that hyperoxic conditions can be maintained for 2 h with the method described. In the lidocaine group none of the pulse oximeters showed a psO2 less than 99%. Our results show significant differences between the three pulse oximeters. Therefore, in contrast to the convention followed in the literatur, the relation between Met-Hb and psO2 under hyperoxic conditions must be described with different formulas for each pulse oximeter as follows: (1) Ohmeda BIOX 3700e: Met-Hb = (101-psO2).0.6 (r = 0.94); (2) Critikon Oxyshuttle: Met-Hb = (101-psO2).0.7 (r = 0.83); (3) Nellcor N 180: Met-Hb = (101-psO2).0.9 (r = 0.92). DISCUSSION. Our results show that it is not possible to describe the connection between Met-Hb and psO2 for all pulse oximeters with only one formula, but it is possible to set up different formulas with good correlations for each of the three pulse oximeters. The reasons for the different sensitivity are probably the different algorithms used by the manufacturers. In spite of the good correlations we can not recommend Met-Hb estimation by pulse oximetry measurement with two wave-lengths, because the distinction of hypoxia and Met-Hb its not possible when hyperoxic conditions are not stable as they were in our controlled study. A low psO2 measured in patients with normal arterial blood gases can be an indication of Met-Hb, but the exact measurement of dyshaemoglobin is only possibly by using a co-oximeter.
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PMID:[The use of pulse oximetry in prilocaine induced methemoglobinemia]. 859 66

Collagen IV networks are present in all metazoans as components of basement membranes that underlie epithelia. They are assembled by the oligomerization of triple-helical protomers, composed of three alpha-chains. The trimeric noncollagenous domains (NC1) of each protomer interact forming a hexamer structure. Upon exposure to acidic pH or denaturants, the hexamer dissociates into monomer and dimer subunits, the latter reflect distinct interactions that reinforce/cross-link the quaternary structure of hexamer. Recently, the cross-link site of the alpha1alpha1alpha2 network was identified, on the basis of x-ray crystal structures at 1.9-A resolution, in which the side chains of Met93 and Lys211 were proposed to be connected by a novel thioether bond (Than, M. E., Henrich, S., Huber, R., Ries, A., Mann, K., Kuhn, K., Timpl, R., Bourenkov, G. P., Bartunik, H. D., and Bode, W. (2002) Proc. Natl. Acad. Sci. U. S. A. 99, 6607-6612); however, at the higher resolution of 1.5 A, we found no evidence for this cross-link (Vanacore, R. M., Shanmugasundararaj, S., Friedman, D. B., Bondar, O., Hudson, B. G., and Sundaramoorthy, M. (2004) J. Biol. Chem. 279, 44723-44730). Given this discrepancy in crystallographic findings, we sought chemical evidence for the location and nature of the reinforcement/cross-link site. Trypsin digestion of monomer and dimer subunits excised a approximately 5,000-Da complex that distinguished dimers from monomers; the complex was characterized by mass spectrometry, Edman degradation, and amino acid composition analyses. The tryptic complex, composed of two peptides of 44 residues derived from two alpha1 NC1 monomers, contained Met93 and Lys211 post-translationally modified to hydroxylysine (Hyl211). Truncation of the tryptic complex with post-proline endopeptidase reduced its size to 14 residues to facilitate characterization by tandem mass spectrometry, which revealed a covalent linkage between Met93 and Hyl211. The novel cross-link, termed S-hydroxylysyl-methionine, reflects at least two post-translational events in its formation: the hydroxylation of Lys211 to Hyl211 within the NC1 domain during the biosynthesis of alpha-chains and the connection of Hyl211 to Met93 between the trimeric NC1 domains of two adjoining triple-helical protomers, reinforcing the stability of collagen IV networks.
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PMID:Identification of S-hydroxylysyl-methionine as the covalent cross-link of the noncollagenous (NC1) hexamer of the alpha1alpha1alpha2 collagen IV network: a role for the post-translational modification of lysine 211 to hydroxylysine 211 in hexamer assembly. 1595 40

We have investigated the sulfilimine covalent link between methionine (Met) and lysine (Lys), recently identified in collagen IV (R. Vanacore, A.-J. L. Ham, M. Voehler, C. R. Sanders, T. P. Conrads, T. D. Veenstra, K. B. Sharpless, P. E. Dawson, B. G. Hudson, Science 2009, 325, 1230), and have explored its stability with respect to both the redox processes and UV radiation by means of advanced computational methods. We have concluded that the bond should be present in a protonated state, (-NH=S-)(+). The bond is characterized by a relatively high standard reduction potential, that is, the bond should not be stable in a typical cell environment; if the sulfilimine bond exists (as suggested by the experiment) then the bond has to be supported by the protein environment. The sulfilimine bond then destabilizes the protein structure with respect to the alternative tertiary structure. We discuss conditions under which the bond could be formed as well as other possible structural arrangements consistent with the Met-Lys stoichiometry; some of the alternative bond motifs are more thermodynamically stable than the sulfilimine bond. We suggest that the character of the Met-Lys contact could be approached via NEXAFS spectroscopy. Finally, we show that the protonation brings photostability to the sulfilimine bond.
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PMID:Novel covalent bond in proteins: calculations on model systems question the bond stability. 2214 75