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  • Articles  (3)
  • crotapotin  (2)
  • sequence homology  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Enzymatic Characterization of a Novel Phospholipase A2 from Crotalus durissus cascavella Rattlesnake (Maracambóia) Venom (2000)
    Springer
    The protein journal 19 (2000), S. 603-607 
    Details
    ISSN: 1573-4943
    Keywords: Crotalus durissus cascavella ; crotoxin ; crotapotin ; PLA2 ; rattlesnake ; venom
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The PLA2 and crotapotin subunits of crotoxin from Crotalus durissus cascavella venom were purified by a combination of HPLC molecular exclusion (Protein Pack 300SW column) and reverse-phase HPLC (RP-HPLC). Tricine SDS—PAGE showed that the PLA2 and crotapotins migrated as single bands with estimated molecular masses of 15 and 9 kDa, respectively. The amino acid composition of the PLA2 showed the presence of 14 half-cysteines and a high content of basic residues (Lys, Arg, His), whereas the crotapotins were rich in hydrophobic, negatively charged residues and half-cysteines. The PLA2 showed allosteric behavior, with maximal activity at pH 8.3 and 35–40°C. The C. d. cascavella PLA2 required Ca2+ for activity, but was inhibited by Cu2+ and Zn2+ and by Cu2+ and Mg2+ in the presence and absence of Ca2+, respectively. Crotapotin (F3) and heparin inhibited the catalytic activity of the PLA2 by acting as allosteric inhibitors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007123329817
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  • 2
    Electronic Resource
    Electronic Resource
    Enzymatic Characterization of a Novel Phospholipase A2 from Crotalus durissus cascavella Rattlesnake (Maracambóia) Venom (2000)
    Springer
    The protein journal 19 (2000), S. 679-684 
    Details
    ISSN: 1573-4943
    Keywords: Crotalus durissus cascavella ; crotoxin ; crotapotin ; PLA2 ; rattlesnake ; venom
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The PLA2 and crotapotin subunits of crotoxin from Crotalus durissus cascavella venom were purified by a combination of high-performance liquid chromatography (HPLC) molecular exclusion (Protein Pack 300SW column) and reverse-phase HPLC (RP-HPLC). Tricine SDS-PAGE showed that the PLA2 and crotapotins migrated as single bands with estimated molecular masses of 15 and 9 kDa, respectively. The amino acid composition of the PLA2 showed the presence of 14 half-cysteines and a high content of basic residues (Lys, Arg, His), whereas the crotapotins were rich in hydrophobic, negatively charged residues and half-cysteines. The PLA2 showed allosteric behavior, with maximal activity at pH 8.3 and 35–40°C. C. d. cascavella PLA2 required Ca2+ for activity but was inhibited by Cu2+ and Zn2+ and by Cu2+ and Mg2+ in the presence and absence of Ca2+, respectively. Crotapotin (F3) and heparin inhibited the catalytic activity of the PLA2 by acting as allosteric inhibitors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007152303179
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Bothropstoxin-I: Amino acid sequence and function (1993)
    Springer
    The protein journal 12 (1993), S. 57-64 
    Details
    ISSN: 1573-4943
    Keywords: Phospholipase A2 ; myotoxin ; bothropstoxin ; B. jararacussu ; sequence homology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The complete amino acid sequence of bothropstoxin-I (BthTX-I), a myotoxin isolated fromBothrops jararacussu snake venom, is reported. The results show that BthTX-I is a Lys49 phospholipase A2 (PLA2)-like protein composed of a single polypeptide chain of 121 amino acid residues (M r=13,720), containing one methionine and 14 half-cystines. Although deprived of any detectable PLA2 activity, BthTX-I reveals a high degree of sequence homology with Asp49-PLA2s and with other Lys49-myotoxins. Critical mutations—such as Leu5 for Phe5; Gln11 for X11; Asn28 for Tyr28; Leu32 for Gly32; Lys49 for Asp49; and Asp71 for Asn71—which are apparently involved with the decreasing or elimination of PLA2 activity, have been detected. The same mutations occurred in myotoxin II fromBothrops asper venom, but five extra changes—namely, Pro90 for Ser90; Gly111 for Asn111; His120 for Tyr120; Phe124 for Leu124; and Pro132 for Ala132—have been found relative to myotoxin II.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024915
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