Search results for "HISTIDINES"

showing 3 items of 3 documents

Endogenous 3-methylhistidine excretion in healthy women and men with reference to muscle protein metabolism.

1984

Presently 3-methylhistidine excretion is widely used for monitoring the metabolic status of patients during different kinds of clinical conditions. Aim of the study was to reconsider its predicative value on the basis of a larger collective of healthy persons and to find a standardization independent from sex. Therefore endogenous 3-methylhistidine release of 40 healthy adults (24 women and 16 men) was measured and related to body weight, body surface area, arm muscle circumference, and nitrogen and creatinine excretion. A positive correlation could be observed only for 3-methylhistidine and creatinine excretion and that to the same extent both for females and males. Assuming that the excre…

AdultMalemedicine.medical_specialtyMedicine (miscellaneous)Renal functionMuscle ProteinsEndogenyBiologyBiochemistryExcretionchemistry.chemical_compoundSex FactorsMyofibrilsInternal medicinemedicineHumansHistidineBody surface areaCreatinineAnthropometryMusclesBody WeightAge FactorsMetabolismMiddle AgedMethylhistidinesProtein catabolismSkinfold ThicknessEndocrinologychemistryCreatinineFemaleMyofibrilFood ScienceZeitschrift fur Ernahrungswissenschaft
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Vitamin A Deficiency Increases Protein Catabolism and Induces Urea Cycle Enzymes in Rats

2010

Chronic vitamin A deficiency induces a substantial delay in the rates of weight and height gain in both humans and experimental animals. This effect has been associated with an impaired nutrient metabolism and loss of body protein. Therefore, we analyzed the effect of vitamin A deficiency on endogenous proteolysis and nitrogen metabolism and its reversibility with all-trans retinoic acid (RA). Male weanling rats, housed in pairs, were pair-fed a vitamin A-deficient (VAD) or control diet until they were 60 d old. A group of deficient rats were further treated with daily intraperitoneal injections of all-trans RA for 10 d. Final body and tissue (i.e. liver and heart) weights were significantl…

MaleVitaminmedicine.medical_specialtyNitrogenMedicine (miscellaneous)TretinoinBiologyAntioxidantsRetinoidschemistry.chemical_compoundInternal medicinemedicineAnimalsUreaMuscle SkeletalTriglyceridesNutrition and DieteticsVitamin A DeficiencyCatabolismRetinolProtein turnoverMethylhistidinesmedicine.diseaseRatsVitamin A deficiencyProtein catabolismEndocrinologyLiverchemistryEnzyme InductionUrea cycleLipid PeroxidationEnergy sourceThe Journal of Nutrition
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Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family

2017

AbstractWe introduce LytU, a short member of the lysostaphin family of zinc-dependent pentaglycine endopeptidases. It is a potential antimicrobial agent for S. aureus infections and its gene transcription is highly upregulated upon antibiotic treatments along with other genes involved in cell wall synthesis. We found this enzyme to be responsible for the opening of the cell wall peptidoglycan layer during cell divisions in S. aureus. LytU is anchored in the plasma membrane with the active part residing in the periplasmic space. It has a unique Ile/Lys insertion at position 151 that resides in the catalytic site-neighbouring loop and is vital for the enzymatic activity but not affecting the …

0301 basic medicineentsyymitantimicrobial compoundsPROTEINchemistry.chemical_compoundCatalytic DomainCELL-WALLBINDINGMultidisciplinaryACTIVE-SITEQRESISTANT STAPHYLOCOCCUS-AUREUSRHydrogen-Ion ConcentrationAnti-Bacterial AgentsZincBiochemistryMedicineHISTIDINESProtein BindingStaphylococcus aureusScienceenzymesBiologyCleavage (embryo)metalloproteinasesArticleCofactorBACILLUS-SUBTILISCell wallStructure-Activity Relationship03 medical and health sciencesEndopeptidasesProtein Interaction Domains and MotifsAmino Acid Sequencestaphylococciantimikrobiset yhdisteetBinding SitesLysostaphinCell MembraneActive siteIsothermal titration calorimetryPeriplasmic spaceVANCOMYCINstafylokokitmetalloproteinaasitMODEL030104 developmental biologyRESOLUTIONchemistryMutationProteolysisLysostaphinbiology.protein1182 Biochemistry cell and molecular biologyPeptidoglycanScientific Reports
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