[HTML][HTML] Identification of the calmodulin-binding domain of recombinant calcium-independent phospholipase A2β: implications for structure and function
CM Jenkins, MJ Wolf, DJ Mancuso… - Journal of Biological …, 2001 - ASBMB
Calcium-independent phospholipase A 2 (iPLA 2) is the major phospholipase A 2 activity in
many cell types, and at least one isoform of this enzyme class is physically and functionally
coupled to calmodulin (CaM) in a reversible calcium-dependent fashion. To identify the
domain in recombinant iPLA 2 β (riPLA 2 β) underlying this interaction, multiple techniques
were employed. First, we identified calcium-activated CaM induced alterations in the kinetics
of proteolytic fragment generation during limited trypsinolysis (ie CaM footprinting). Tryptic …
many cell types, and at least one isoform of this enzyme class is physically and functionally
coupled to calmodulin (CaM) in a reversible calcium-dependent fashion. To identify the
domain in recombinant iPLA 2 β (riPLA 2 β) underlying this interaction, multiple techniques
were employed. First, we identified calcium-activated CaM induced alterations in the kinetics
of proteolytic fragment generation during limited trypsinolysis (ie CaM footprinting). Tryptic …