title: [Structuro-functional characteristics of aldolase from rabbit muscles in diabetes].
abstract: The structural peculiarities of rabbit muscle aldolase accompanying enhancement of the aldolase activity in diabetes are described from the data of tryptophan phosphorescence at the room temperature and fluorescence polarization. It is shown that the pathology-concomitant conformational changes occur in both the hydrophobic part and NAD-binding site of the enzyme. The character of the structural changes in the hydrophobic part of the protein in diabetes and an increase in the enzymic activity are similar to that observed in normal aldolase after its interaction with NADH and are believed to be associated with the enhancement of the rigidity in the Trp-147 environment.
authors.forename: Iu V
authors.initials: IuV
authors.lastname: Chumachenko
authors.forename: A I
authors.initials: AI
authors.lastname: Sytnik
authors.forename: V M
authors.initials: VM
authors.lastname: Mazhul'
authors.forename: V P
authors.initials: VP
authors.lastname: Nikol'skaia
mesh_terms: D000818:Animals; D003921:Diabetes Mellitus, Experimental / Q000201:enzymology*; D005634:Fructose-Bisphosphate Aldolase / Q000032:analysis*; D009132:Muscles / Q000201:enzymology*; D009243:NAD; D011487:Protein Conformation; D011817:Rabbits; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000032:analysis
chemical_list: D009243:NAD; D014364:Tryptophan; D005634:Fructose-Bisphosphate Aldolase
vernacular_title: Strukturno-funktsional'nye osobennosti al'dolazy myshts krolikov pri diabete.