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Volumn 124, Issue 2, 1999, Pages 181-186

Effect of neutral salts on activity and stability of transglutaminase from scallop adductor muscle

Author keywords

Adductor muscle; Marine invertebrate; Mollusks; Neutral salts; Salt stimulation; Scallop; Sodium chloride; Transglutaminase; Wound healing

Indexed keywords

PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; SODIUM CHLORIDE;

EID: 0032867548     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(99)00111-X     Document Type: Article
Times cited : (14)

References (24)
  • 1
    • 0028946284 scopus 로고
    • Transglutaminase-catalyzed matrix cross-linking in differentiating cartilage: Identification of osteonectin as a major glutaminyl substrate
    • Aeschlimann D, Kaupp O, Paulsson M. Transglutaminase-catalyzed matrix cross-linking in differentiating cartilage: identification of osteonectin as a major glutaminyl substrate. J Cell Biol 1995;129:881-92.
    • (1995) J Cell Biol , vol.129 , pp. 881-892
    • Aeschlimann, D.1    Kaupp, O.2    Paulsson, M.3
  • 2
    • 0023213422 scopus 로고
    • High-performance liquid Chromatographic assay of transglutaminase and its application to the purification on human erythrocyte transglutaminase and platelet factor XIII
    • Ando Y, Imamura S, Yamagata Y, Kikuchi T, Murachi T, Kannagi R. High-performance liquid Chromatographic assay of transglutaminase and its application to the purification on human erythrocyte transglutaminase and platelet factor XIII. J Biochem 1987;101:1331-7.
    • (1987) J Biochem , vol.101 , pp. 1331-1337
    • Ando, Y.1    Imamura, S.2    Yamagata, Y.3    Kikuchi, T.4    Murachi, T.5    Kannagi, R.6
  • 3
    • 0032434398 scopus 로고    scopus 로고
    • Monolayer formation and DNA synthesis of the outer epithelial cells from pearl oyster mantle in coculture with amebocytes
    • Awaji M, Suzuki T. Monolayer formation and DNA synthesis of the outer epithelial cells from pearl oyster mantle in coculture with amebocytes. In vitro Cell Dev Biol Anim 1998;34:486-91.
    • (1998) In Vitro Cell Dev Biol Anim , vol.34 , pp. 486-491
    • Awaji, M.1    Suzuki, T.2
  • 4
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin RL. How Hofmeister ion interactions affect protein stability. Biophys J 1996;71:2056-63.
    • (1996) Biophys J , vol.71 , pp. 2056-2063
    • Baldwin, R.L.1
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0029841641 scopus 로고    scopus 로고
    • Structural and functional aspects of chloride binding to Alteromonas haloplanctis α-amylase
    • Feller G, Bussy O, Houssier C, Gerday C. Structural and functional aspects of chloride binding to Alteromonas haloplanctis α-amylase. J Biol Chem 1996;271:23836-41.
    • (1996) J Biol Chem , vol.271 , pp. 23836-23841
    • Feller, G.1    Bussy, O.2    Houssier, C.3    Gerday, C.4
  • 7
    • 0018816617 scopus 로고
    • Transglutaminases
    • Folk JE. Transglutaminases. Annu Rev Biochem 1980;49:517-31.
    • (1980) Annu Rev Biochem , vol.49 , pp. 517-531
    • Folk, J.E.1
  • 8
    • 0041341327 scopus 로고
    • Functional properties of succinylated and acetylated soy protein
    • Franzen KL, Kinsella JE. Functional properties of succinylated and acetylated soy protein. J Agric Food Chem 1976;24:788-95.
    • (1976) J Agric Food Chem , vol.24 , pp. 788-795
    • Franzen, K.L.1    Kinsella, J.E.2
  • 9
    • 0026338017 scopus 로고
    • Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg CS, Birckbichler PJ, Rice RH. Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues. FASEB J 1991;5:3071-7.
    • (1991) FASEB J , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 11
    • 0030772527 scopus 로고    scopus 로고
    • Effect of pH, temperature, and alcohols on the remarkable activation of thermolysin by salts
    • Inouye K, Lee S, Nambu K, Tonomura B. Effect of pH, temperature, and alcohols on the remarkable activation of thermolysin by salts. J Biochem 1997;122:358-64.
    • (1997) J Biochem , vol.122 , pp. 358-364
    • Inouye, K.1    Lee, S.2    Nambu, K.3    Tonomura, B.4
  • 12
    • 0031848311 scopus 로고    scopus 로고
    • Effects of nitration and animation of tyrosyl residues in thermolysin on its hydrolytic activity and its remarkable activation by salts
    • Inouye K, Lee S, Tonomura B. Effects of nitration and animation of tyrosyl residues in thermolysin on its hydrolytic activity and its remarkable activation by salts. J Biochem 1998;124:72-8.
    • (1998) J Biochem , vol.124 , pp. 72-78
    • Inouye, K.1    Lee, S.2    Tonomura, B.3
  • 13
    • 0001176908 scopus 로고    scopus 로고
    • Purification and characterization of transglutaminase from Japanese oyster (Crassostrea gigas)
    • Kumazawa Y, Sano K, Seguro K, Yasueda H, Nio N, Motoki M. Purification and characterization of transglutaminase from Japanese oyster (Crassostrea gigas). J Agric Food Chem 1997;45:604-10.
    • (1997) J Agric Food Chem , vol.45 , pp. 604-610
    • Kumazawa, Y.1    Sano, K.2    Seguro, K.3    Yasueda, H.4    Nio, N.5    Motoki, M.6
  • 15
    • 0011878828 scopus 로고
    • Haemostatic mechanisms in the invertebrata
    • Needham AE. Haemostatic mechanisms in the invertebrata. Symp Zool Soc Lond 1970;27:19-44.
    • (1970) Symp Zool Soc Lond , vol.27 , pp. 19-44
    • Needham, A.E.1
  • 16
    • 0031452970 scopus 로고    scopus 로고
    • Partial purification and characterization of six transglutaminases from ordinary muscles of various fishes and marine invertebrates
    • Nozawa H, Mamegoshi S, Seki N. Partial purification and characterization of six transglutaminases from ordinary muscles of various fishes and marine invertebrates. Comp Biochem Physiol 1997;118B:313-7.
    • (1997) Comp Biochem Physiol , vol.118 B , pp. 313-317
    • Nozawa, H.1    Mamegoshi, S.2    Seki, N.3
  • 17
    • 0025219629 scopus 로고
    • Non-proteolytic activation of cellular protransglutaminase (placenta macrophage Factor XIII)
    • Polgar J, Hidasi V, Muszbek L. Non-proteolytic activation of cellular protransglutaminase (placenta macrophage Factor XIII). Biochem J 1990;267:557-60.
    • (1990) Biochem J , vol.267 , pp. 557-560
    • Polgar, J.1    Hidasi, V.2    Muszbek, L.3
  • 18
    • 0003111941 scopus 로고
    • Inorganic ions
    • Presser CL, editor. Philadelphia: W.B. Saunders
    • Presser CL. Inorganic ions. In: Presser CL, editor. Comparative Animal Physiology. Philadelphia: W.B. Saunders, 1973:79-110.
    • (1973) Comparative Animal Physiology , pp. 79-110
    • Presser, C.L.1
  • 19
    • 0010413698 scopus 로고
    • Wound healing system in molluscs
    • Mori K, Kamiya H, editors. Tokyo: Kouseisha Kouseikaku
    • Suzuki T, Awaji M. Wound healing system in molluscs. In: Mori K, Kamiya H, editors. Defense Mechanisms in Aquatic Animals (Japanese). Tokyo: Kouseisha Kouseikaku, 1995:83-95.
    • (1995) Defense Mechanisms in Aquatic Animals (Japanese) , pp. 83-95
    • Suzuki, T.1    Awaji, M.2
  • 20
    • 0027050283 scopus 로고
    • An involucrin-like protein in hepatocytes serves as a substrate for tissue transglutaminase during apoptosis
    • Tarcsa E, Kedei N, Thomazy V, Fesus L. An involucrin-like protein in hepatocytes serves as a substrate for tissue transglutaminase during apoptosis. J Biol Chem 1992;267:25648-51.
    • (1992) J Biol Chem , vol.267 , pp. 25648-25651
    • Tarcsa, E.1    Kedei, N.2    Thomazy, V.3    Fesus, L.4
  • 21
    • 0027445392 scopus 로고
    • Horseshoe crab transglutaminase
    • Tokunaga F, Iwanaga S. Horseshoe crab transglutaminase. Methods Enzymol 1993;223:378-88.
    • (1993) Methods Enzymol , vol.223 , pp. 378-388
    • Tokunaga, F.1    Iwanaga, S.2
  • 23
    • 0030594809 scopus 로고    scopus 로고
    • Transglutaminases: Purification and activity assays
    • Wilhelm B, Meinhardt A, Seitz J. Transglutaminases: purification and activity assays. J Chromatogr 1996;684:163-77.
    • (1996) J Chromatogr , vol.684 , pp. 163-177
    • Wilhelm, B.1    Meinhardt, A.2    Seitz, J.3
  • 24
    • 13044256242 scopus 로고
    • Electrostatic interactions
    • New York: Dover Publications
    • William PJ. Electrostatic interactions. In: Catalysis in Chemistry and Enzymology. New York: Dover Publications, 1987:358-92.
    • (1987) Catalysis in Chemistry and Enzymology , pp. 358-392
    • William, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.