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1.
PLoS One ; 17(6): e0265416, 2022.
Article in English | MEDLINE | ID: mdl-35737690

ABSTRACT

To give an insight into the different manifestations of leprosy and their biological consequences in the Avar Age of the Hungarian Duna-Tisza Interfluve, two cases from the 7th-century-CE osteoarchaeological series of Kiskundorozsma-Daruhalom-dulo II (Hungary; n = 94) were investigated. Based on the macromorphology of the bony changes indicative of Hansen's disease, KD271 (a middle-aged male) and KD520 (a middle-aged female) represent the two extremes of leprosy. KD271 appears to have an advanced-stage, long-standing near-lepromatous or lepromatous form of the disease, affecting not only the rhinomaxillary region but also both upper and lower limbs. This has led to severe deformation and disfigurement of the involved anatomical areas of the skeleton, resulting in his inability to perform the basic activities of daily living, such as eating, drinking, grasping, standing or walking. The skeleton of KD520 shows no rhinomaxillary lesions and indicates the other extreme of leprosy, a near-tuberculoid or tuberculoid form of the disease. As in KD271, Hansen's disease has resulted in disfigurement and disability of both of the lower limbs of KD520; and thus, the middle-aged female would have experienced difficulties in standing, walking, and conducting occupational physical activities. KD271 and KD520 are amongst the very few published cases with leprosy from the Avar Age of the Hungarian Duna-Tisza Interfluve, and the only examples with detailed macromorphological description and differential diagnoses of the observed leprous bony changes. The cases of these two severely disabled individuals, especially of KD271 -who would have required regular and substantial care from others to survive-imply that in the Avar Age community of Kiskundorozsma-Daruhalom-dulo II there was a willingness to care for people in need.


Subject(s)
Activities of Daily Living , Leprosy , Benzodiazepines , Diagnosis, Differential , Female , Humans , Hungary , Leprosy/diagnosis , Male , Middle Aged , Sulfur
2.
Int J Lepr Other Mycobact Dis ; 51(1): 64-71, 1983 Mar.
Article in English | MEDLINE | ID: mdl-6345413

ABSTRACT

Mycobacterium lepraemurium was cultivated on Ogawa egg-yolk medium and its respiratory activities using several substrates were investigated. Glycerol and succinate were oxidized at a slow rate by the cell-free extracts prepared from in vitro grown Hawaiian and Keishicho strains of M. lepraemurium. None of the other intermediates of the glycolysis cycle as well as of the tricarboxylic acid cycle was oxidized by the whole cell suspensions or cell-free extracts. Likewise, many sulfur compounds such as cystine, mercaptosuccinate, monothioglycerol, thioacetate, etc., were inactive. However, sulfhydryl compounds such as L-cysteine, D-cysteine, DL-cysteine, dithioerythritol, dithiothritol, and DL-penicillamine were actively oxidized. Yeast extract was also readily oxidized by cell suspensions of in vitro grown M. lepraemurium. Tween 80 was very poorly oxidized by whole cell suspensions but the cell-free preparations catalyzed an active oxidation of Tween 80. While bovine serum albumin was oxidized at a slow rate by cell-free extracts, egg albumin was inactive. The thiol-binding agents, p-hydroxymercuribenzoate and N-ethylmaleimide were effective inhibitors of succinate and NADH oxidation, thus indicating the involvement of sulfhydryl compounds in the metabolism of M. lepraemurium.


Subject(s)
Mycobacterium lepraemurium/metabolism , Oxidation-Reduction , In Vitro Techniques , Sulfur/metabolism
3.
J Biol Chem ; 256(17): 9216-20, 1981 Sep 10.
Article in English | MEDLINE | ID: mdl-6267066

ABSTRACT

Two N-1 type iron-sulfur clusters in NADH-ubiquinone oxidoreductase (Complex I, EC 1.6.5.3) were potentiometrically resolved: one was titrated as a component with a midpoint oxidation-reduction potential of -335 mV at pH 8.0, and with an n-value equal to one; the other as an extremely low midpoint potential component (Em 8.0 less than -500 mV). These two clusters are tentatively assigned to N-1b and N-1a, respectively. Cluster N-1b is completely reducible with NADH and has a spin concentration of about 0.8/FMN. Its EPR spectrum can be simulated as a single rhombic component with principal g values of 2.019, 1.937, and 1.922, which correspond to the Center 1 reported earlier by Orme-Johnson, N. R., Hansen, R. E., and Beinert, H. (1974) J. Biol. Chem. 249, 1922-1927. At extremely low oxidation-reduction potentials (less than -450 mV), additional EPR signals emerge with apparent g values of gz = 2.03, gy = 1.95, and gx = 1.91, which we assign to cluster N-1a. It is difficult, however, to simulate the detailed spectral line shape of this component as a single rhombic component, suggesting some degree of protein modification or interaction with a neighboring oxidation-reduction component. EPR spectra of soluble NADH dehydrogenase, containing 5-6 g atoms of non-heme iron and 5-6 mol of acid-labile sulfide/mol of FMN, were examined. Signals from at least two iron-sulfur species could be distinguished in the NADH-reduced form: one of an N-1b type spectrum; the other of a spectrum with g values of 2.045, 1.95, and 1.87 (total of about 0.5 spin equivalents/FMN). This is the first example of an N-1 type signal detected in isolated soluble NADH dehydrogenase.


Subject(s)
Cytochrome Reductases/metabolism , Iron-Sulfur Proteins/metabolism , Iron/analysis , Metalloproteins/metabolism , NADH Dehydrogenase/metabolism , NADH, NADPH Oxidoreductases/metabolism , Quinone Reductases/metabolism , Sulfur/analysis , Binding Sites , Electron Spin Resonance Spectroscopy , Flavin Mononucleotide/analysis , Kinetics , NAD(P)H Dehydrogenase (Quinone) , Oxidation-Reduction , Potentiometry , Protein Binding , Protein Conformation
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