2019
DOI: 10.1016/j.cbpb.2019.110337
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Biochemical characterization of recombinant Penaeus vannamei trypsinogen

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Cited by 3 publications
(4 citation statements)
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“…This tetra-Asp sequence together with Asp217 (chymo#) has been involved in an inhibitory function for trypsin-mediated trypsinogen activation (autoactivation), by an electrostatic repulsion between Asp217 (chymo#) and the tetra-aspartate (Nemoda & Sahin-Tóth, 2007). Therefore, the corresponding trypsinogen of the Mc-TryL protease likely has an increased autoactivation rate in comparison with other non-crustacean trypsins in a similar manner as we have recently described for the P. vannamei trypsinogen (Guerrero-Olazarán et al, 2019), although with slight differences due to the lack of Arg or Lys at the end of the propeptide. Since the storage of active trypsin is a risk of tissue damage through hydrolysis of autologous protein, M. carcinus must possess a tightly regulated mechanism for controlling activation until needed for a precise function similar to other crustaceans.…”
Section: Discussionsupporting
confidence: 57%
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“…This tetra-Asp sequence together with Asp217 (chymo#) has been involved in an inhibitory function for trypsin-mediated trypsinogen activation (autoactivation), by an electrostatic repulsion between Asp217 (chymo#) and the tetra-aspartate (Nemoda & Sahin-Tóth, 2007). Therefore, the corresponding trypsinogen of the Mc-TryL protease likely has an increased autoactivation rate in comparison with other non-crustacean trypsins in a similar manner as we have recently described for the P. vannamei trypsinogen (Guerrero-Olazarán et al, 2019), although with slight differences due to the lack of Arg or Lys at the end of the propeptide. Since the storage of active trypsin is a risk of tissue damage through hydrolysis of autologous protein, M. carcinus must possess a tightly regulated mechanism for controlling activation until needed for a precise function similar to other crustaceans.…”
Section: Discussionsupporting
confidence: 57%
“…Since the storage of active trypsin is a risk of tissue damage through hydrolysis of autologous protein, M. carcinus must possess a tightly regulated mechanism for controlling activation until needed for a precise function similar to other crustaceans. The control of trypsin activity in crustacea is a fine-tuning mechanism that involves the continuous regulation of trypsin activity through zymogen storage, secretion and activation like frequent feeder species (Sainz et al, 2004;Guerrero-Olazarán et al, 2019), with a main role of trypsin inhibitors for controlling trypsin activity and/or trypsinogen activation (García-Carreño, Carrillo & Navarrete del Toro, 1999;De Albuquerque-Cavalcanti, García-Carreño & Navarrete del Toro, 2002;Guerrero-Olazarán et al, 2019).…”
Section: Discussionmentioning
confidence: 99%
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“…Esto indicaría que a pesar de que la actividad de las enzimas alcalinas se vio afectada negativamente por el uso del preservante, las tripsinas se encuentran activas en mayor proporción en la composición enzimática total. Por otro lado, la abrupta reducción de la actividad alcalina en los langostinos tratados con MBS podría deberse a que este compuesto ha provocado la ruptura y/o reordenamiento de enlaces disulfuro en las enzimas provocando su inactivación (Zhang y Sun 2008; Guerrero-Olazarán et al 2019). Esto último concuerda con los resultados obtenidos por Friedman y Gumbmann (1986), quienes detectaron una reducción en la actividad inhibidora de tripsinas de harina de soja en presencia de sulfito de sodio.…”
Section: Proteasas áCidas Proteasas Alcalinasunclassified