[ POLYMORPHISME DES HYDROLASES LYSOSOMALES CHEZ L’ABEILLE (APIS MELLIFERA L.) A BUKAVU ET SES ENVIRONS (SUD-KIVU, REPUBLIQUE DEMOCRATIQUE DU CONGO) ]
Volume 31, Issue 1, June 2017, Pages 94–116
Dieudonné C.T. BAKENGA MATABARO1, Alexandre MBAYA NTUMBULA2, and Simone WATTIAUX-DE CONINCK3
1 Institut Supérieur Pédagogique de Bukavu, ISP/Bukavu, RD Congo
2 Université Pédagogique National de Kinshasa, UPN, RD Congo
3 Université de Namur, Belgium
Original language: French
Copyright © 2017 ISSR Journals. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
The polymorphism of lysosoma ß- galactosidase (EC. 3.2.1.23) and N- acetylglucosaminidase (EC. 3.2.1.49) has been established taking into account the variation of their specific activities at both the larval, pupal and adult stages. These activities have been decreased from the larva stage (22.03 ± 4.3 nmoles/min/mg of protein) to the adult stage (5.30 ± 1.27 nmoles/min/mg of protein) via the pupal stage (20.4 ± 1.78 nmoles/min/mg of protein). The N- acetylglucosaminidase activity has been about 10 times as higher as that of β-galactosidase. That activity of the N- acetylglucosaminidase is 200.88 ± 31.39 nmoles/min/mg of protein for larvae, 115.00 ± 21.02 nmoles/min/mg of protein for pupas and 9.48 ± 2.23 nmoles/min/mg of protein for adults. The activities of both 2 enzymes have followed the MICHAELIS-MENTEN law as they were positively linear as well in function of the enzyme concentration and the incubation time as in function of the substrate concentration. The temperature has influenced their respective activities according to ARRHENIUS law, the Q10 being around 2. The cathepsine C (EC. 3.4.14.1) activities have been equal to 2.03 ± 1.18, 0.95 ± 0.54 and 0.76 ± 0.39 nmoles/min/mg of protein for larvae, pupas and adults, respectively. For the acid phosphatase (EC. 3.1.3.2), the activities have been equal to 6.29 ± 2.87, 6.89 ± 2.69 and 8.51 ± 4.51 nmoles/min/mg of protein for larvae, pupas and adults, respectively. These activities are weak comparatively to those of the former two glycosidases at the 3 development stages of Apis mellifera L. Conversely, the venom acid phosphatase has been very active (25.32 ± 6.94 nmoles/min/mg of protein), an activity almost 20 times higher than that of both cathepsine C, β-galactosidase and N-acetylglucosaminidase. The β-galactosidase and N-acetylglucosaminidase from larvae and pupas have all the characteristics of lysosoma enzymes. They have a maximum activity at acidic pH, i.e. 5 for the β-galactosidase and 6 for the N-acetylglucosaminidase, and present a latency property that is annihilated by detergents. A fraction of their activity being sedimentable in the used experimental conditions, these 2 glycosidases are most likely lysosoma acid hydrolases and indicate the presence of lysosomes in Apis mellifera L. In addition, as their activities vary during the bee development stages, it becomes evident the 2 glycosidases are involved in the bee metamorphosis and are thus polymorphic in Apis mellifera L. Another enzyme, i.e. the hyaluronidase (EC. 3.2.1.35; MW 37 kDa), has been identified in the bee venom.
Author Keywords: Apis mellifera L., polymorphism, lysosome, enzyme.
Volume 31, Issue 1, June 2017, Pages 94–116
Dieudonné C.T. BAKENGA MATABARO1, Alexandre MBAYA NTUMBULA2, and Simone WATTIAUX-DE CONINCK3
1 Institut Supérieur Pédagogique de Bukavu, ISP/Bukavu, RD Congo
2 Université Pédagogique National de Kinshasa, UPN, RD Congo
3 Université de Namur, Belgium
Original language: French
Copyright © 2017 ISSR Journals. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract
The polymorphism of lysosoma ß- galactosidase (EC. 3.2.1.23) and N- acetylglucosaminidase (EC. 3.2.1.49) has been established taking into account the variation of their specific activities at both the larval, pupal and adult stages. These activities have been decreased from the larva stage (22.03 ± 4.3 nmoles/min/mg of protein) to the adult stage (5.30 ± 1.27 nmoles/min/mg of protein) via the pupal stage (20.4 ± 1.78 nmoles/min/mg of protein). The N- acetylglucosaminidase activity has been about 10 times as higher as that of β-galactosidase. That activity of the N- acetylglucosaminidase is 200.88 ± 31.39 nmoles/min/mg of protein for larvae, 115.00 ± 21.02 nmoles/min/mg of protein for pupas and 9.48 ± 2.23 nmoles/min/mg of protein for adults. The activities of both 2 enzymes have followed the MICHAELIS-MENTEN law as they were positively linear as well in function of the enzyme concentration and the incubation time as in function of the substrate concentration. The temperature has influenced their respective activities according to ARRHENIUS law, the Q10 being around 2. The cathepsine C (EC. 3.4.14.1) activities have been equal to 2.03 ± 1.18, 0.95 ± 0.54 and 0.76 ± 0.39 nmoles/min/mg of protein for larvae, pupas and adults, respectively. For the acid phosphatase (EC. 3.1.3.2), the activities have been equal to 6.29 ± 2.87, 6.89 ± 2.69 and 8.51 ± 4.51 nmoles/min/mg of protein for larvae, pupas and adults, respectively. These activities are weak comparatively to those of the former two glycosidases at the 3 development stages of Apis mellifera L. Conversely, the venom acid phosphatase has been very active (25.32 ± 6.94 nmoles/min/mg of protein), an activity almost 20 times higher than that of both cathepsine C, β-galactosidase and N-acetylglucosaminidase. The β-galactosidase and N-acetylglucosaminidase from larvae and pupas have all the characteristics of lysosoma enzymes. They have a maximum activity at acidic pH, i.e. 5 for the β-galactosidase and 6 for the N-acetylglucosaminidase, and present a latency property that is annihilated by detergents. A fraction of their activity being sedimentable in the used experimental conditions, these 2 glycosidases are most likely lysosoma acid hydrolases and indicate the presence of lysosomes in Apis mellifera L. In addition, as their activities vary during the bee development stages, it becomes evident the 2 glycosidases are involved in the bee metamorphosis and are thus polymorphic in Apis mellifera L. Another enzyme, i.e. the hyaluronidase (EC. 3.2.1.35; MW 37 kDa), has been identified in the bee venom.
Author Keywords: Apis mellifera L., polymorphism, lysosome, enzyme.
Abstract: (french)
Le polymorphisme de la ß- galactosidase (EC. 3.2.1.23) et de la N- acétylglucosaminidase (EC. 3.2.1.49) lysosomales a été établi tenant compte de la variation de leurs activités spécifiques aux stades larvaire, pupal et adulte. Ces activités ont été réduites du stade larvaire (22,03 ± 4,9 nmoles/min/mg de protéine) au stade adulte (5,30 ± 1,27 ? nmoles/min/mg de protéine), en passant par le stade pupal (20,4 ± 1,78 nmoles/min/mg de protéine). L’activité de la N- acétylglucosaminidase est environ 10 fois plus élevée que celle de la β-galactosidase. Elle est de (200,88 ± 31,39 nmoles/min/mg de protéine pour les larves, 115,00 ± 21,02 nmoles/min/mg de protéines pour les pupes et 9,48 ± 2,23 nmoles/min/mg de protéine pour les adultes). Les activités respectives de ces 2 enzymes ont suivi la loi de MICHAELIS-MENTEN, car elles sont positivement linéaires en fonction de la concentration en enzyme, du temps d’incubation et en fonction de la concentration en substrat. La température a influencé leurs activités respectives selon la Loi d’ARRHENIUS, le Q10 ayant une valeur qui avoisine 2. Les activités de la cathepsine C (EC. 3.4.14.1) ont été de 2,03 ± 1,18 ; 0,95 ± 0,54 et 0,76 ± 039 nmoles/min/mg de protéine pour les larves, les pupes et les adultes, respectivement. Celles de la phosphatase acide (EC. 3.1.3.2.) équivalent respectivement à 6,29 ± 2,87 ; 6,89 ± 2,69 et 8,51 ± 4,51 nmoles/min/mg de protéine pour les larves, les pupes et les adultes. Ces activités sont faibles comparativement à celles des 2 glycosidases précitées aux 3 stades de développement de Apis mellifera. La phosphatase acide est par contre très active au niveau du venin (25,32 ± 6,94 nmoles/min/mg de protéines), son activité étant environ 20 fois supérieure à celles de la cathepsine C, de la β galactosidase et de la N- acétylglucosaminidase. La ß-galactosidase et la N-acétylglucosaminidase des larves et pupes ont toutes les caractéristiques des enzymes lysosomales. Elles ont une activité maximale à pH acide, soit 5 pour la ß-galactosidase et 6 pour la N-acétylglucosaminidase, et présentent une propriété de latence qui est annulée par les détergents. Une partie de leur activité pouvant sédimenter dans les conditions expérimentales utilisées, ces 2 glycosidases sont donc très probablement des hydrolases acides lysosomales et signalent la présence de lysosomes chez Apis mellifera L. En plus, comme leurs activités varient pendant les étapes de développement, il devient évident que les 2 glycosidases sont impliquées dans la métamorphose de l’abeille et sont donc polymorphiques chez Apis mellifera L. Une autre enzyme, l’hyaluronidase (EC. 3.2.1.35 ; PM 37 kDa), a été en plus identifiée dans le venin d’abeille.
Author Keywords: Apis mellifera L., polymorphisme, lysosome, enzyme.
How to Cite this Article
Dieudonné C.T. BAKENGA MATABARO, Alexandre MBAYA NTUMBULA, and Simone WATTIAUX-DE CONINCK, “Polymorphism of lysosomal hydrolases in bee (Apis mellifera L.) from BUKAVU and its surroundings (South-KIVU, Democratic Republic of Congo),” International Journal of Innovation and Scientific Research, vol. 31, no. 1, pp. 94–116, June 2017.
