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The structural isomerisation of human-muscle adenylate kinase as studied by ¹H-nuclear magnetic resonance

Kalbitzer, Hans Robert and Marquetant, R. and Rösch, P. and Schirmer, R H. (1982) The structural isomerisation of human-muscle adenylate kinase as studied by ¹H-nuclear magnetic resonance. European journal of biochemistry= EJB: The FEBS journal 126 (3), pp. 531-536.

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Abstract

Human muscle adenylate kinase (ATP:AMP phosphotransferase, EC 2.7.4.3.) was studied by 1H-nuclear magnetic resonance spectroscopy. The C-2 and C-4 proton resonances of the active-center histidine His-36 could be identified; the pK of His-36 was determined as 6.1. The pK of His-189 is very low (4.9) although it is located at the surface of the protein. Other resonance lines are discussed in ...

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Item Type:Article
Date:1982
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
6291931PubMed ID
Classification:
NotationType
Adenylate Kinase/isolation & purificationMESH
AnimalsMESH
HumansMESH
Hydrogen-Ion ConcentrationMESH
Magnetic Resonance SpectroscopyMESH
Muscles/enzymologyMESH
Phosphotransferases/isolation & purificationMESH
Species SpecificityMESH
StereoisomerismMESH
Structure-Activity RelationshipMESH
SwineMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:02 Sep 2010 06:38
Last Modified:02 Sep 2010 06:38
Item ID:16432
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