[Ca-inhibited binding of melittin with parvalbumin. A new role for parvalbumins?].
It was found that pike parvalbumins pI 4.2 and 5.0 bind amphiphilic peptide melittin extracted from bee venom in an extraordinary Ca-dependent manner: in apo-state the protein forms a tight equimolar complex with melittin (Ka = 10(6) M-1 at 18 degrees C); in Ca- (and Mg-) loaded state it does not take place. Heating of the protein up to temperatures above the denaturation temperature of apo-parvalbumin does not change the stoichiometry of the complex but increases its association constant by an order of magnitude (Ka = 1.2.10(7) M-1 at 44 degrees C). Isolated Ca-binding domain of parvalbumin, 38-108, retains the ability for Ca-inhibited binding of equimolar quantities of melittin. The possible function of parvalbumin in vivo is suggested: Ca-inhibited interactions with some intracellular components.
Permiakov
E A
EA
Medvedkin
V N
VN
Koreneĭchuk
G A
GA
Kostrzhevskaia
E G
EG
Murzin
A G
AG
D000818:Animals; D001514:Bee Venoms / Q000378:metabolism*; D001516:Bees; D002118:Calcium / Q000494:pharmacology*; D005399:Fishes; D008555:Melitten / Q000037:antagonists & inhibitors / Q000378:metabolism*; D009124:Muscle Proteins / Q000378:metabolism*; D010320:Parvalbumins / Q000378:metabolism*; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence
D001514:Bee Venoms; D009124:Muscle Proteins; D010320:Parvalbumins; D008555:Melitten; D002118:Calcium
Ingibiruemoe ionami Ca sviazyvanie melittina parval'buminom. Novaia rol' dlia parval'buminov?