[The role of the N-terminal fragment of troponin T in the interaction with troponin-tropomyosin complex components of the heart].
Bovine heart troponin T was hydrolyzed at the single cysteine residue. This procedure resulted in two peptides--a short N-terminal peptide (40-50 amino acid residues) and a long C-terminal peptide (240 amino acid residues). The C-terminal peptide was purified to homogeneity by ion-exchange chromatography; its properties were compared to those of intact troponin T. Data from circular dichroism spectroscopy suggest that the short N-terminal peptide cleavage was unaccompanied by any conspicuous changes in the secondary structure of the large C-terminal peptide of troponin T. Unlike intact troponin T, its C-terminal peptide can interact with troponin C in the presence of Ca2+. Data from affinity chromatography demonstrated that troponin I and tropomyosin more strongly interacted with native troponin T than with its C-terminal peptide. It is concluded that the short N-terminal peptide (40-50 residues) plays an essential role in cardiac troponin T interaction with troponin and tropomyosin components.
Verin
A D
AD
Gusev
N B
NB
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D009132:Muscles / Q000032:analysis; D009206:Myocardium / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D011817:Rabbits; D014335:Tropomyosin / Q000032:analysis*; D014336:Troponin / Q000032:analysis*; D019209:Troponin C; D020107:Troponin T
D000596:Amino Acids; D010446:Peptide Fragments; D014335:Tropomyosin; D014336:Troponin; D019209:Troponin C; D020107:Troponin T
Izuchenie roli N-kontsevogo fragmenta troponina T vo vzaimodeĭstvii s komponentami troponintropomiozinovogo kompleksa serdtsa.