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J. Biol. Chem., Vol. 259, Issue 20, 12489-12494, 10, 1984
T Sasaki, T Kikuchi, N Yumoto, N Yoshimura and T Murachi
Homogeneous porcine calpain (Ca2+-dependent cysteine proteinase) was found
to hydrolyze a variety of peptides and synthetic substrates. Leu-
Trp-Met-Arg-Phe-Ala, eledoisin-related peptide, alpha-neoendorphin,
angiotensin I, luteinizing hormone-releasing hormone, neurotensin,
dynorphin, glucagon, and oxidized insulin B chain were cleaved with a
general preference for a Tyr, Met, or Arg residue in the P1 position
preceded by a Leu or Val residue in the P2 position. No great difference in
specificity was found between low-Ca2+-requiring calpain I and
high-Ca2+-requiring calpain II. 4-Methylcoumaryl-7-amide (MCA) derivatives
having a Leu(or Val)-Met(or Tyr)-MCA or a Leu-Lys-MCA sequence were also
cleaved by either calpain I or calpain II with preference for Leu over Val
by a factor of 9 to 16. Calpains I and II showed similar but not identical
kinetic behavior for individual substrates. The Km and kcat values ranged
from 0.23 to 7.08 mM and 0.062 to 0.805 s-1 for the calpains, while kcat/Km
values for the calpains were only 1/433 to 1/5 of those for papain with a
given substrate. With succinyl-Leu-Met(or Tyr)-MCA, calpains I and II were
half-maximally activated at 12 and 260 microM Ca2+, respectively, and
competitively inhibited by leupeptin (Ki = 0.32 microM for I and 0.43
microM for II) or antipain (Ki = 1.41 microM for I and 1.45 microM for II).
Thus, this is the first report describing the specificity and kinetics of
calpains I and II.
Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates
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