TY - JOUR
T1 - Penaeus vannamei isotrypsins
T2 - Purification and characterization
AU - Sainz, Juan Carlos
AU - García-Carreño, Fernando L.
AU - Hernández-Cortés, Patricia
N1 - Funding Information:
This work was supported by Consejo Nacional de Ciencia y Tecnologı́a of Mexico (CONACYT grants J33750-N and 27371-B) to P. Hernández and CONACYT fellowship 153559 to J.C. Sainz. At CIBNOR, M.A. Navarrete del Toro and A.P. Sierra-Beltrán provided technical assistance and editing staff modified the English text.
PY - 2004/6
Y1 - 2004/6
N2 - Three isotrypsins from digestive gland of Penaeus vannamei were purified and characterized by molecular, biochemical and kinetic parameters. Purified isotrypsins A, B, and C are glycoproteins with molecular masses between 30.2 and 32.9 kDa, and, therefore similar to other trypsins. The isoelectric points are anionic and different among the three isotrypsins: pH 3.5 for isotrypsin A, pH 3.0 for isotrypsin B, and pH 4.5 for isotrypsin C. Differences in the NH 2-terminal amino acid sequences allowed us to define three different protein entities that match isotrypsins previously deduced by cDNA. Isoform C has higher physiological efficiency and specific activity, lower Km, and requires higher concentrations of Ca+2 to reach the same activity as the other two isotrypsins.
AB - Three isotrypsins from digestive gland of Penaeus vannamei were purified and characterized by molecular, biochemical and kinetic parameters. Purified isotrypsins A, B, and C are glycoproteins with molecular masses between 30.2 and 32.9 kDa, and, therefore similar to other trypsins. The isoelectric points are anionic and different among the three isotrypsins: pH 3.5 for isotrypsin A, pH 3.0 for isotrypsin B, and pH 4.5 for isotrypsin C. Differences in the NH 2-terminal amino acid sequences allowed us to define three different protein entities that match isotrypsins previously deduced by cDNA. Isoform C has higher physiological efficiency and specific activity, lower Km, and requires higher concentrations of Ca+2 to reach the same activity as the other two isotrypsins.
KW - Invertebrate trypsin
KW - Isoenzymes
KW - Penaeus vannamei
UR - http://www.scopus.com/inward/record.url?scp=2942607953&partnerID=8YFLogxK
U2 - 10.1016/j.cbpc.2004.03.002
DO - 10.1016/j.cbpc.2004.03.002
M3 - Artículo
SN - 1096-4959
VL - 138
SP - 155
EP - 162
JO - Comparative Biochemistry and Physiology -- Part B: Biochemistry and
JF - Comparative Biochemistry and Physiology -- Part B: Biochemistry and
IS - 2
ER -