Properties of N-acetyl-β-glucosaminidase in the masseter muscle of the mouse
The present study was undertaken to clarify various characteristics of N-acetyl-β-glucosaminidase (NAG) in the masseter muscle of the mouse. The pH optimum of NAG in tissue homogenate was 4.3, and Km value for p-nitrophenyl-N-acetyl-β-glucosaminide was 0.98 mM. By means of isoelertric focusing, NAG...
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| Published in | Japanese Journal of Oral Biology Vol. 32; no. 1; pp. 1 - 9 |
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| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English Japanese |
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Japan
Japanese Association for Oral Biology
01.02.1990
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| ISSN | 0385-0137 |
| DOI | 10.2330/joralbiosci1965.32.1 |
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| Abstract | The present study was undertaken to clarify various characteristics of N-acetyl-β-glucosaminidase (NAG) in the masseter muscle of the mouse. The pH optimum of NAG in tissue homogenate was 4.3, and Km value for p-nitrophenyl-N-acetyl-β-glucosaminide was 0.98 mM. By means of isoelertric focusing, NAG in the masseter muscle was separated into four enzymes (NAG I-IV). The isoelectric points were: I, 4.9; II, 6.4; III, 7.2 and IV, 8.7. The pH optima of NAG I-IV ranged from 4.2 to 4.4, and Km values from 0.61 to 0.83 mM. The molecular weights of I, II, III and IV were 135, 000, 120, 000, 135, 000 and 110, 000, respectively. Studies on heat stability showed that NAG I and IV were slightly labile as compared with II and III. The activities of NAG I-IV were dose dependently inhibited by both N-acetyl-glucosamine and N-acetyl-galactosamine. Both Ag+ and Hg2+ ions caused a marked inhibition on activities of NAG I-IV. |
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| AbstractList | The present study was undertaken to clarify various characteristics of N-acetyl-beta-glucosaminidase (NAG) in the masseter muscle of the mouse. The pH optimum of NAG in tissue homogenate was 4.3, and Km value for p-nitrophenyl-N-acetyl-beta-glucosaminide was 0.98 mM. By means of isoelectric focusing. NAG in the masseter muscle was separated into four enzymes (NAG I-IV). The isoelectric points were: I, 4.9; II, 6.4; III, 7.2 and IV, 8.7. The pH optima of NAG I-IV ranged from 4.2 to 4.4, and Km values from 0.61 to 0.83 mM. The molecular weights of I, II, III and IV were 135,000, 120,000, 135,000 and 110,000, respectively. Studies on heat stability showed that NAG I and IV were slightly labile as compared with II and III. The activities of NAG I-IV were dose dependently inhibited by both N-acetyl-glucosamine and N-acetyl-galactosamine. Both Ag and Hg2+ ions caused a marked inhibition on activities of NAG I-IV. The present study was undertaken to clarify various characteristics of N-acetyl-β-glucosaminidase (NAG) in the masseter muscle of the mouse. The pH optimum of NAG in tissue homogenate was 4.3, and Km value for p-nitrophenyl-N-acetyl-β-glucosaminide was 0.98 mM. By means of isoelertric focusing, NAG in the masseter muscle was separated into four enzymes (NAG I-IV). The isoelectric points were: I, 4.9; II, 6.4; III, 7.2 and IV, 8.7. The pH optima of NAG I-IV ranged from 4.2 to 4.4, and Km values from 0.61 to 0.83 mM. The molecular weights of I, II, III and IV were 135, 000, 120, 000, 135, 000 and 110, 000, respectively. Studies on heat stability showed that NAG I and IV were slightly labile as compared with II and III. The activities of NAG I-IV were dose dependently inhibited by both N-acetyl-glucosamine and N-acetyl-galactosamine. Both Ag+ and Hg2+ ions caused a marked inhibition on activities of NAG I-IV. The present study was undertaken to clarify various characteristics of N-acetyl-beta-glucosaminidase (NAG) in the masseter muscle of the mouse. The pH optimum of NAG in tissue homogenate was 4.3, and Km value for p-nitrophenyl-N-acetyl-beta-glucosaminide was 0.98 mM. By means of isoelectric focusing. NAG in the masseter muscle was separated into four enzymes (NAG I-IV). The isoelectric points were: I, 4.9; II, 6.4; III, 7.2 and IV, 8.7. The pH optima of NAG I-IV ranged from 4.2 to 4.4, and Km values from 0.61 to 0.83 mM. The molecular weights of I, II, III and IV were 135,000, 120,000, 135,000 and 110,000, respectively. Studies on heat stability showed that NAG I and IV were slightly labile as compared with II and III. The activities of NAG I-IV were dose dependently inhibited by both N-acetyl-glucosamine and N-acetyl-galactosamine. Both Ag and Hg2+ ions caused a marked inhibition on activities of NAG I-IV.The present study was undertaken to clarify various characteristics of N-acetyl-beta-glucosaminidase (NAG) in the masseter muscle of the mouse. The pH optimum of NAG in tissue homogenate was 4.3, and Km value for p-nitrophenyl-N-acetyl-beta-glucosaminide was 0.98 mM. By means of isoelectric focusing. NAG in the masseter muscle was separated into four enzymes (NAG I-IV). The isoelectric points were: I, 4.9; II, 6.4; III, 7.2 and IV, 8.7. The pH optima of NAG I-IV ranged from 4.2 to 4.4, and Km values from 0.61 to 0.83 mM. The molecular weights of I, II, III and IV were 135,000, 120,000, 135,000 and 110,000, respectively. Studies on heat stability showed that NAG I and IV were slightly labile as compared with II and III. The activities of NAG I-IV were dose dependently inhibited by both N-acetyl-glucosamine and N-acetyl-galactosamine. Both Ag and Hg2+ ions caused a marked inhibition on activities of NAG I-IV. |
| Author | Hiramatsu, Masahiko Ueda, Kazuya Sato, Akinao Ui, Kazuhiko Murayama, Makoto Kashimata, Masanori Minami, Naomi |
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| References | 17) Weissmann, B. and Friederici, D.: Occurrence of a mammalian α-N-acetyl-D-galactosaminidase. Biochim. Biophys. Acta 117: 498-499, 1966. 22) Hultberg, B., Öckerman, P.A. and Norden, N.E.: Isoenzymes of four acid hydrolases in human kidney and urine. Clin. Chim. Acta 52: 239-243, 1974. 6) Seyaman Y. and Yamakawa, T.: Multiple components of β-N-acetylhexosaminidase from equine kindney: their action on glycolipids and allied oligosaccharides. J. Biochem. 75: 495-507, 1974. 7) Wiktorowicz, J.E., Awasthi, Y.C., Kurosky, A. and Srivastava, S.K.: Purification and properties human kidney-cortex hexosaminidases A and B. Biochem. J. 165: 49-53, 1977. 8) Kobayashi, S., Hosoi, K. and Ueha, T.: Purification and properties of β-N-acetyl-hexosaminidase from mouse submandibular gland. Arch. Oral Biol. 25: 753-758, 1980. 12) Lojda, Z. and Gutmann, E.: Histochemistry of some acid hydrolases in striated muscle of the rat. Histochemistry 49: 337-342, 1976. 20) Price, R.G. and Dance, N.: The cellular distribution of some rat-kindney glycosidases. Biochem. J. 105: 877-883, 1967. 1) 鈴木伊豆美, 櫛田秀雄, 志田半三郎: 哺乳動物のグリコシダーゼについて (第1報) -N-アセチル-α-D-ヘキソサミニダーゼおよびN-アセチル-β-D-ヘキソサミニダーゼについて-. 生化学40: 838-850, 1968. 9) 浅井計征: ラット唾液腺N-アセチルヘキソサミニダーゼの分離とその性状. 歯科医学51: 97-113,1988. 15) Hiramatsu, M., Murayama, M., Kashimata, M., Sato, A., Maeda, N., Kumegawa, M. and Minami, N.: Elevation of lysosomal enzyme activities in the masseter muscle of muscular dystrophic mice. Jpn. J. Oral Biol. 30: 713-716, 1988. 2) Sandhoff, K. and Wassle, W.: Anreicherung und charakterisierung zweier formen der menschlichen N-acetyl-β-D-hexosaminidase. Hoppe-Seyler's Z. Physiol. Chem. 352: 1119-1133, 1971. 18) Srivastava, S.K., Yoshida, A., Awasthi, Y.C. and Beutler, E.: Studies on human β-D.N. acetylhexosaminidase. II. Kinetic and structural properties. J. Biol. Chem. 249: 2049-2053, 1974. 19) Khar, A. and Anand, S.R.: Studies on the glycosidases of semen: purification and properties of β-N-acetylglucosaminidase from bull sperm. Biochim. Biophys. Acta 483: 141-151, 1977. 16) Murayama, M., Hiramatsu, M., Kashimata, M., Sato, A., Ueda, K., Maeda, N., Kumegawa, M. and Minami, N.: Developmental change in activity of N acetyl-β-glucosaminidase and comparison of its multiple enzyme activities in the masseter muscle of normal and dystrophic mice. Jpn. J. Oral Biol. 31: 609-612, 1989. 3) Wenger, D.A., Okada, S. and O'Brien, J.S.: Studies on the substrate specificity of hexosaminidase A and B from liver. Arch. Biochem. Biophys. 153: 116-129, 1972. 10) Pugh, D. and Walker, P.G.: Histochemical localization of β-glucuronidase and Nacetyl-β-glucosaminidase. J. Histochem. Cytochem. 9: 105-106, 1961. 11) Pugh, D. and Walker, P.G.: The localization of N-acetyl-β-glucosaminidase in tissues. J. Histochem. Cytochem. 9: 242-250, 1961. 4) Robinson, D. and Stirling, J.L.: N-Acetyl-β-glucosaminidases in human spleen. Biochem. J. 107: 321-327, 1968. 5) Verpoorte, J.A.: Purification of two β-N-acetyl-D-glucosaminidases from beef spleen. J. Biol. Chem. 247: 4787-4793, 1972. 14) Salminen, A. and Marjornäki, V.: Phosphomannosyl receptors of lysosomal enzymes in cardiac and skeletal muscles of young and old mice. Comp. Biochem. Physiol. 82B: 259-262, 1985. 13) Libelius, R., Lundquist, I., Tagerud, S. and Thesleff, S.: Endocytosis and lysosomal enzyme activities in dystrophic muscle: the effect of denervation. Acta Physiol. Scand. 113: 259-261, 1981. 21) 千住紀, 矢沢直行, 長谷川俊二, 石井康夫, 鵜沢龍一, 五味邦英, 細谷純一郎: N-Acetyl-β-D-glucosaminidase (NAG) isozymeに関する基礎的研究. 臨床病理33: 1407-1412, 1985. |
| References_xml | – reference: 6) Seyaman Y. and Yamakawa, T.: Multiple components of β-N-acetylhexosaminidase from equine kindney: their action on glycolipids and allied oligosaccharides. J. Biochem. 75: 495-507, 1974. – reference: 7) Wiktorowicz, J.E., Awasthi, Y.C., Kurosky, A. and Srivastava, S.K.: Purification and properties human kidney-cortex hexosaminidases A and B. Biochem. J. 165: 49-53, 1977. – reference: 18) Srivastava, S.K., Yoshida, A., Awasthi, Y.C. and Beutler, E.: Studies on human β-D.N. acetylhexosaminidase. II. Kinetic and structural properties. J. Biol. Chem. 249: 2049-2053, 1974. – reference: 22) Hultberg, B., Öckerman, P.A. and Norden, N.E.: Isoenzymes of four acid hydrolases in human kidney and urine. Clin. Chim. Acta 52: 239-243, 1974. – reference: 17) Weissmann, B. and Friederici, D.: Occurrence of a mammalian α-N-acetyl-D-galactosaminidase. Biochim. Biophys. Acta 117: 498-499, 1966. – reference: 20) Price, R.G. and Dance, N.: The cellular distribution of some rat-kindney glycosidases. Biochem. J. 105: 877-883, 1967. – reference: 9) 浅井計征: ラット唾液腺N-アセチルヘキソサミニダーゼの分離とその性状. 歯科医学51: 97-113,1988. – reference: 5) Verpoorte, J.A.: Purification of two β-N-acetyl-D-glucosaminidases from beef spleen. J. Biol. Chem. 247: 4787-4793, 1972. – reference: 8) Kobayashi, S., Hosoi, K. and Ueha, T.: Purification and properties of β-N-acetyl-hexosaminidase from mouse submandibular gland. Arch. Oral Biol. 25: 753-758, 1980. – reference: 13) Libelius, R., Lundquist, I., Tagerud, S. and Thesleff, S.: Endocytosis and lysosomal enzyme activities in dystrophic muscle: the effect of denervation. Acta Physiol. Scand. 113: 259-261, 1981. – reference: 11) Pugh, D. and Walker, P.G.: The localization of N-acetyl-β-glucosaminidase in tissues. J. Histochem. Cytochem. 9: 242-250, 1961. – reference: 12) Lojda, Z. and Gutmann, E.: Histochemistry of some acid hydrolases in striated muscle of the rat. Histochemistry 49: 337-342, 1976. – reference: 1) 鈴木伊豆美, 櫛田秀雄, 志田半三郎: 哺乳動物のグリコシダーゼについて (第1報) -N-アセチル-α-D-ヘキソサミニダーゼおよびN-アセチル-β-D-ヘキソサミニダーゼについて-. 生化学40: 838-850, 1968. – reference: 3) Wenger, D.A., Okada, S. and O'Brien, J.S.: Studies on the substrate specificity of hexosaminidase A and B from liver. Arch. Biochem. Biophys. 153: 116-129, 1972. – reference: 15) Hiramatsu, M., Murayama, M., Kashimata, M., Sato, A., Maeda, N., Kumegawa, M. and Minami, N.: Elevation of lysosomal enzyme activities in the masseter muscle of muscular dystrophic mice. Jpn. J. Oral Biol. 30: 713-716, 1988. – reference: 21) 千住紀, 矢沢直行, 長谷川俊二, 石井康夫, 鵜沢龍一, 五味邦英, 細谷純一郎: N-Acetyl-β-D-glucosaminidase (NAG) isozymeに関する基礎的研究. 臨床病理33: 1407-1412, 1985. – reference: 2) Sandhoff, K. and Wassle, W.: Anreicherung und charakterisierung zweier formen der menschlichen N-acetyl-β-D-hexosaminidase. Hoppe-Seyler's Z. Physiol. Chem. 352: 1119-1133, 1971. – reference: 10) Pugh, D. and Walker, P.G.: Histochemical localization of β-glucuronidase and Nacetyl-β-glucosaminidase. J. Histochem. Cytochem. 9: 105-106, 1961. – reference: 14) Salminen, A. and Marjornäki, V.: Phosphomannosyl receptors of lysosomal enzymes in cardiac and skeletal muscles of young and old mice. Comp. Biochem. Physiol. 82B: 259-262, 1985. – reference: 4) Robinson, D. and Stirling, J.L.: N-Acetyl-β-glucosaminidases in human spleen. Biochem. J. 107: 321-327, 1968. – reference: 19) Khar, A. and Anand, S.R.: Studies on the glycosidases of semen: purification and properties of β-N-acetylglucosaminidase from bull sperm. Biochim. Biophys. Acta 483: 141-151, 1977. – reference: 16) Murayama, M., Hiramatsu, M., Kashimata, M., Sato, A., Ueda, K., Maeda, N., Kumegawa, M. and Minami, N.: Developmental change in activity of N acetyl-β-glucosaminidase and comparison of its multiple enzyme activities in the masseter muscle of normal and dystrophic mice. Jpn. J. Oral Biol. 31: 609-612, 1989. |
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| Snippet | The present study was undertaken to clarify various characteristics of N-acetyl-β-glucosaminidase (NAG) in the masseter muscle of the mouse. The pH optimum of... The present study was undertaken to clarify various characteristics of N-acetyl-beta-glucosaminidase (NAG) in the masseter muscle of the mouse. The pH optimum... |
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| SubjectTerms | Acetylglucosaminidase - antagonists & inhibitors Acetylglucosaminidase - chemistry Animals Hydrogen-Ion Concentration Isoelectric Focusing masseter muscle Masseter Muscle - enzymology Mice Molecular Weight mouse N-Acetyl-β-glucosaminidase |
| Title | Properties of N-acetyl-β-glucosaminidase in the masseter muscle of the mouse |
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