[Isolation of the calcium-binding domain of carp parvalbumin].
Carp parvalbumin has two calcium-binding domains with a similar three-dimensional structure. Using the tryptic hydrolysis at the arginine residue in position 75, it was possible to split off one calcium-binding domain. All lysine residues were protected by maleic groups which were removed at the final stage. The domain (with a peptide thirty-three residues) isolated by ion-exchange chromatography and gel filtration does not have a secondary structure in a solution and is unable to bind calcium.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D002347:Carps / Q000378:metabolism*; D002352:Carrier Proteins; D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D002852:Chromatography, Ion Exchange; D002942:Circular Dichroism; D003530:Cyprinidae / Q000378:metabolism*; D009124:Muscle Proteins; D010320:Parvalbumins; D011485:Protein Binding; D014357:Trypsin
D000596:Amino Acids; D002352:Carrier Proteins; D009124:Muscle Proteins; D010320:Parvalbumins; D014357:Trypsin; D002118:Calcium
Vydelenie kal'tsiĭsviazyvaiushchego domena parval'bumina karpa.