Comparative analysis of β-hexosaminidase and acid phosphatase from Hydra vulgaris Ind-Pune, H. vulgaris Naukuchiatal and H. magnipapillata sf-1: Localization studies of acid phosphatase and β-hexosaminidase from H. vulgaris Ind-Pune

Publication date: Available online 17 October 2019Source: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular BiologyAuthor(s): Rohit Sai Reddy Konada, Lakshmi Surekha Krishnapati, Ashapogu Venugopal, Chung-Hung Lin, Siva Kumar NadimpalliAbstractThe present report describes a comprehensive study on comparative biochemical characterization of two lysosomal enzymes, acid phosphatase and β-hexosaminidase in three different strains of Hydra; Hydra vulgaris Ind-Pune, H. vulgaris Naukuchiatal and H. magnipapillata sf-1 (self-feeder-1). Since morphology and habitat of Hydra effect lysosomal enzymes and their response to environmental pollutants, it would be interesting to identify them in different Hydra strains so as to use them as toxicity testing. Preliminary studies revealed a differential expression of acid phosphatase, β-hexosaminidase and β-glucuronidase in three Hydra strains. Expression of all three lysosomal enzymes in H. vulgaris Ind-Pune was low in comparison to H. vulgaris Naukuchiatal and H. magnipapillata sf-1, while their expression is comparable in H. vulgaris Naukuchiatal and H. magnipapillata sf-1. The Michaelis-Menten (KM) values for lysosomal β-hexosaminidase using 4-nitrophenyl N-acetyl-β-D-glucosaminide as substrate were found to be 1.3 mM, 1.1 mM and 0.8 mM, respectively for H. vulgaris Ind-Pune, H. vulgaris Naukuchiatal and H. magnipapillata sf-1. For acid phosphatase using 4-nitrophenyl-phosphate as substrate, the KM values...
Source: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology - Category: Molecular Biology Source Type: research