메뉴 건너뛰기




Volumn 1, Issue , 2004, Pages 29-32

Chymosin

Author keywords

[No Author keywords available]

Indexed keywords


EID: 33847218149     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-079611-3.50013-6     Document Type: Chapter
Times cited : (8)

References (50)
  • 2
    • 0026482515 scopus 로고
    • Production of prochymosin, pepsinogen and progastricsin, and their cellular and intracellular localization in bovine abomasal mucosa
    • A. Andrén (1992) Production of prochymosin, pepsinogen and progastricsin, and their cellular and intracellular localization in bovine abomasal mucosa. Scand. J. Clin. Lab. Invest. 52(suppl. 210), 59-64.
    • (1992) Scand. J. Clin. Lab. Invest. , vol.52 , pp. 59-64
    • Andrén, A.1
  • 4
    • 0021766654 scopus 로고
    • Kinetics of the action of chymosin (rennin) on some peptide bond of bovine β-casein
    • C. Carles and B. Ribadeau-Dumas (1984) Kinetics of the action of chymosin (rennin) on some peptide bond of bovine β-casein. Biochemistry 23 6839-6843.
    • (1984) Biochemistry , vol.23 , pp. 6839-6843
    • Carles, C.1    Ribadeau-Dumas, B.2
  • 5
    • 0021839138 scopus 로고
    • s1 -casein
    • C. Carles and B. Ribadeau-Dumas (1985) Kinetics of the action of chymosin (rennin) on a peptide bond of bovine α s1 -casein. FEBS Lett. 185 282-286.
    • (1985) FEBS Lett. , vol.185 , pp. 282-286
    • Carles, C.1    Ribadeau-Dumas, B.2
  • 6
    • 0034633936 scopus 로고    scopus 로고
    • Functional implications of disulfide bond, Cys206-Cys210, in recombinant prochymosin (chymosin)
    • H. Chen, G. Zhang, Y. Zhang, Y. Dong and K. Yang (2000) Functional implications of disulfide bond, Cys206-Cys210, in recombinant prochymosin (chymosin). Biochemistry 39 12140-12148.
    • (2000) Biochemistry , vol.39 , pp. 12140-12148
    • Chen, H.1    Zhang, G.2    Zhang, Y.3    Dong, Y.4    Yang, K.5
  • 7
    • 0032102577 scopus 로고    scopus 로고
    • Site-specific mutations of calf chymosin B which influence milk clotting activity
    • S. Chitpinityol, D. Goode and M.J.C. Crabbe (1998) Site-specific mutations of calf chymosin B which influence milk clotting activity. Food Chem. 62 133-139.
    • (1998) Food Chem. , vol.62 , pp. 133-139
    • Chitpinityol, S.1    Goode, D.2    Crabbe, M.J.C.3
  • 8
    • 0023812807 scopus 로고
    • Structure and mechanism of formation of recombinant-derived chymosin C
    • D.E. Danley and K.F. Geoghegan (1988) Structure and mechanism of formation of recombinant-derived chymosin C. J. Biol. Chem. 263 9785-9789.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9785-9789
    • Danley, D.E.1    Geoghegan, K.F.2
  • 9
    • 84884890678 scopus 로고
    • De la présure
    • J.B. Deschamps (1840) De la présure. J. Pharmacol. 26 412-420.
    • (1840) J. Pharmacol. , vol.26 , pp. 412-420
    • Deschamps, J.B.1
  • 11
    • 0013868033 scopus 로고
    • A review on prorennin and rennin
    • B. Foltmann (1966) A review on prorennin and rennin. C.R. Trav. Lab. Carlsberg 35 143-231.
    • (1966) C.R. Trav. Lab. Carlsberg , vol.35 , pp. 143-231
    • Foltmann, B.1
  • 12
    • 0000232655 scopus 로고
    • Prochymosin and chymosin (prorennin and rennin)
    • B. Foltmann (1970) Prochymosin and chymosin (prorennin and rennin). Methods Enzymol. 19 421-436.
    • (1970) Methods Enzymol. , vol.19 , pp. 421-436
    • Foltmann, B.1
  • 13
    • 0026497631 scopus 로고
    • Chymosin. A short review on foetal and neonatal gastric proteases
    • B. Foltmann (1992) Chymosin. A short review on foetal and neonatal gastric proteases. Scand. J. Clin. Lab. Invest. 52(suppl. 210), 65-79.
    • (1992) Scand. J. Clin. Lab. Invest. , vol.52 , pp. 65-79
    • Foltmann, B.1
  • 14
    • 0008050549 scopus 로고
    • General and molecular aspects of rennets
    • P.F. Fox (Eds), London: Chapman & Hall
    • B. Foltmann (1993) General and molecular aspects of rennets. P.F. Fox (Eds) Cheese: Chemistry, Physics and Microbiology 1 London: Chapman & Hall 37-68.
    • (1993) Cheese: Chemistry, Physics and Microbiology , vol.1 , pp. 37-68
    • Foltmann, B.1
  • 15
    • 0343626604 scopus 로고
    • Gastric proteinases and their zymogens. Phylogenetic and developmental aspects
    • P. Mildner,B. Ries (Eds), Oxford: Pergamon
    • B. Foltmann and N.H. Axelsen (1980) Gastric proteinases and their zymogens. Phylogenetic and developmental aspects. P. Mildner,B. Ries (Eds) Enzyme Regulation and Mechanism of Action Oxford: Pergamon 271-280.
    • (1980) Enzyme Regulation and Mechanism of Action , pp. 271-280
    • Foltmann, B.1    Axelsen, N.H.2
  • 18
    • 0021793875 scopus 로고
    • Detection of proteases by clotting of casein after gel electrophoresis
    • B. Foltmann, P.B. Szecsi and N.I. Tarasova (1985) Detection of proteases by clotting of casein after gel electrophoresis. Anal. Biochem. 146 353-360.
    • (1985) Anal. Biochem. , vol.146 , pp. 353-360
    • Foltmann, B.1    Szecsi, P.B.2    Tarasova, N.I.3
  • 20
    • 0035021776 scopus 로고    scopus 로고
    • A basic residue at position 36p of the propeptide is not essential for the correct folding and subsequent autocatalytic activation of prochymosin
    • A. Francky, B.M. Francky, B. Strukelj, K. Gruden, A. Ritonja, I. Krizaj, I. Kregar, R.H. Pain and J. Pungercar (2001) A basic residue at position 36p of the propeptide is not essential for the correct folding and subsequent autocatalytic activation of prochymosin. Eur. J. Biochem. 268 2362-2368.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2362-2368
    • Francky, A.1    Francky, B.M.2    Strukelj, B.3    Gruden, K.4    Ritonja, A.5    Krizaj, I.6    Kregar, I.7    Pain, R.H.8    Pungercar, J.9
  • 21
    • 0029097938 scopus 로고
    • Transcription of embryonic chick pepsinogen gene is affected by mesenchymal signals through its 5′-flanking region
    • K. Fukuda, H. Saiga and S. Yasugi (1995) Transcription of embryonic chick pepsinogen gene is affected by mesenchymal signals through its 5′-flanking region. Adv. Exp. Med. Biol. 362 125-129.
    • (1995) Adv. Exp. Med. Biol. , vol.362 , pp. 125-129
    • Fukuda, K.1    Saiga, H.2    Yasugi, S.3
  • 22
    • 0025374191 scopus 로고
    • The three-dimensional structure of recombinant bovine chymosin at 2.3Å resolution
    • G.L. Gilliland, E.L. Winborne, J. Nachman and A. Wlodawer (1990) The three-dimensional structure of recombinant bovine chymosin at 2.3Å resolution. Proteins 8 82-101.
    • (1990) Proteins , vol.8 , pp. 82-101
    • Gilliland, G.L.1    Winborne, E.L.2    Nachman, J.3    Wlodawer, A.4
  • 23
    • 0030054003 scopus 로고    scopus 로고
    • Post X-ray crystallographic studies of chymosin: the existence of two structural forms and the regulation of activation with the histidine-proline cluster of κ-casein
    • E. Gustchina, L. Rumsch, L. Ginodman, P. Majer and N. Andreeva (1996) Post X-ray crystallographic studies of chymosin: the existence of two structural forms and the regulation of activation with the histidine-proline cluster of κ-casein. FEBS Lett. 399 60-62.
    • (1996) FEBS Lett. , vol.399 , pp. 60-62
    • Gustchina, E.1    Rumsch, L.2    Ginodman, L.3    Majer, P.4    Andreeva, N.5
  • 24
    • 0038524682 scopus 로고
    • Om mjölk-ystningen och de dervid verksamma fermenterna i magslemhinnan
    • O. Hammarsten (1872) Om mjölk-ystningen och de dervid verksamma fermenterna i magslemhinnan. Ups. Läkarefören. Förhandl. 8 63-86.
    • (1872) Ups. Läkarefören. Förhandl. , vol.8 , pp. 63-86
    • Hammarsten, O.1
  • 25
    • 0002874342 scopus 로고    scopus 로고
    • The production, action and application of rennet and coagulants
    • B.A. Law (Eds), Sheffield: Sheffield Academic Press
    • M. Harboe and P. Budtz (1999) The production, action and application of rennet and coagulants. B.A. Law (Eds) Technology of Cheesemaking Sheffield: Sheffield Academic Press 33-65.
    • (1999) Technology of Cheesemaking , pp. 33-65
    • Harboe, M.1    Budtz, P.2
  • 27
    • 0023954680 scopus 로고
    • Molecular cloning and the nucleotide sequence of cDNA for embryonic chicken pepsinogen: phylogenetic relationship with prochymosin
    • K. Hayashi, K. Agata, M. Mochii, S. Yasugi, G. Eguchi and T. Mizuno (1988) Molecular cloning and the nucleotide sequence of cDNA for embryonic chicken pepsinogen: phylogenetic relationship with prochymosin. J. Biochem. (Tokyo) 103 290-296.
    • (1988) J. Biochem. (Tokyo) , vol.103 , pp. 290-296
    • Hayashi, K.1    Agata, K.2    Mochii, M.3    Yasugi, S.4    Eguchi, G.5    Mizuno, T.6
  • 29
    • 0022449861 scopus 로고
    • Cloning and structural analysis of the calf prochymosin gene
    • M. Hidaka, K. Sasaki, T. Uozumi and T. Beppu (1986) Cloning and structural analysis of the calf prochymosin gene. Gene 43 197-203.
    • (1986) Gene , vol.43 , pp. 197-203
    • Hidaka, M.1    Sasaki, K.2    Uozumi, T.3    Beppu, T.4
  • 30
    • 84944118072 scopus 로고
    • Chymase
    • E. Bamann,K. Myrbäck (Eds), Leipzig: G. Thieme Verlag
    • H. Holter (1941) Chymase. E. Bamann,K. Myrbäck (Eds) Die Methoden der Fermentforschung 2 Leipzig: G. Thieme Verlag 2081-2090.
    • (1941) Die Methoden der Fermentforschung , vol.2 , pp. 2081-2090
    • Holter, H.1
  • 32
    • 0022643093 scopus 로고
    • Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution
    • M.N.G. James and A.R. Sielecki (1986) Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution. Nature 319 33-38.
    • (1986) Nature , vol.319 , pp. 33-38
    • James, M.N.G.1    Sielecki, A.R.2
  • 33
    • 0020491878 scopus 로고
    • Isolation and partial characterization of prochymosin and chymosin from cat
    • T. Jensen, N.H. Axelsen and B. Foltmann (1982) Isolation and partial characterization of prochymosin and chymosin from cat. Biochim. Biophys. Acta 705 249-256.
    • (1982) Biochim. Biophys. Acta , vol.705 , pp. 249-256
    • Jensen, T.1    Axelsen, N.H.2    Foltmann, B.3
  • 34
    • 0034033897 scopus 로고    scopus 로고
    • New world monkey pepsinogen A and C, and prochymosins. Purification, characterization of enzymatic properties, cDNA cloning, and molecular evolution
    • T. Kageyama (2000) New world monkey pepsinogen A and C, and prochymosins. Purification, characterization of enzymatic properties, cDNA cloning, and molecular evolution. J. Biochem. (Tokyo) 127 761-770.
    • (2000) J. Biochem. (Tokyo) , vol.127 , pp. 761-770
    • Kageyama, T.1
  • 35
    • 0034719408 scopus 로고    scopus 로고
    • Molecular cloning of neonate/infant-specific pepsinogens from rat stomach mucosa and their expressional change during development
    • T. Kageyama, M. Ichinose, S. Tsukada-Kato, M. Omata, Y. Narita, A. Moriyama and S. Yonezawa (2000) Molecular cloning of neonate/infant-specific pepsinogens from rat stomach mucosa and their expressional change during development. Biochem. Biophys. Res. Commun. 267 806-812.
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 806-812
    • Kageyama, T.1    Ichinose, M.2    Tsukada-Kato, S.3    Omata, M.4    Narita, Y.5    Moriyama, A.6    Yonezawa, S.7
  • 36
    • 84884884299 scopus 로고
    • Notes on the mode of action of rennin and fibrin-ferment
    • A.S. Lea and W.L. Dickinson (1890) Notes on the mode of action of rennin and fibrin-ferment. J. Physiol. 11 307-311.
    • (1890) J. Physiol. , vol.11 , pp. 307-311
    • Lea, A.S.1    Dickinson, W.L.2
  • 37
    • 0020383582 scopus 로고
    • Molecular cloning and characterization of double-stranded cDNA coding for bovine chymosin
    • D. Moir, J.-I. Mao, J.W. Schumm, G.F. Vovis, B.L. Alford and A. Taunton-Rigby (1982) Molecular cloning and characterization of double-stranded cDNA coding for bovine chymosin. Gene 19 127-138.
    • (1982) Gene , vol.19 , pp. 127-138
    • Moir, D.1    Mao, J.-I.2    Schumm, J.W.3    Vovis, G.F.4    Alford, B.L.5    Taunton-Rigby, A.6
  • 38
    • 0025935211 scopus 로고
    • X-ray analysis of aspartic proteinases. IV. Structure and refinement at 2.2Å resolution of bovine chymosin
    • M. Newman, M. Safro, C. Frazao, G. Kahn, A. Zdanov, I.J. Tickle, T.J. Blundell and N. Andreeva (1991) X-ray analysis of aspartic proteinases. IV. Structure and refinement at 2.2Å resolution of bovine chymosin. J. Mol. Biol. 221 1295-1309.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1295-1309
    • Newman, M.1    Safro, M.2    Frazao, C.3    Kahn, G.4    Zdanov, A.5    Tickle, I.J.6    Blundell, T.J.7    Andreeva, N.8
  • 39
    • 0027484178 scopus 로고
    • Activation of porcine pepsinogen A
    • F.S. Nielsen and B. Foltmann (1993) Activation of porcine pepsinogen A. Eur. J. Biochem. 217 137-142.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 137-142
    • Nielsen, F.S.1    Foltmann, B.2
  • 40
    • 0025032718 scopus 로고
    • Structure of the human genomic region homologous to the bovine prochymosin-encoding gene
    • T. Örd, M. Kolmer, R. Villems and M. Saarma (1990) Structure of the human genomic region homologous to the bovine prochymosin-encoding gene. Gene 91 241-246.
    • (1990) Gene , vol.91 , pp. 241-246
    • Örd, T.1    Kolmer, M.2    Villems, R.3    Saarma, M.4
  • 42
    • 0016762041 scopus 로고
    • Amino-acid sequence of the peptide segment liberated during activation of prochymosin (prorennin)
    • V.B. Pedersen and B. Foltmann (1975) Amino-acid sequence of the peptide segment liberated during activation of prochymosin (prorennin). Eur. J. Biochem. 55 95-103.
    • (1975) Eur. J. Biochem. , vol.55 , pp. 95-103
    • Pedersen, V.B.1    Foltmann, B.2
  • 43
  • 47
    • 84944052932 scopus 로고
    • On the presence of a milk-curdling ferment (pexin) in the gastric mucous membrane of vertebrates
    • J.W. Warren (1897) On the presence of a milk-curdling ferment (pexin) in the gastric mucous membrane of vertebrates. J. Exp. Med. 2 475-492.
    • (1897) J. Exp. Med. , vol.2 , pp. 475-492
    • Warren, J.W.1
  • 48
    • 52849103783 scopus 로고    scopus 로고
    • Analysis of the disulfide bonding pattern between domain sequences of recombinant prochymosin solubilized from inclusion bodies
    • C. Wei, H. Chen, Y. Zhang and K. Yang (2000) Analysis of the disulfide bonding pattern between domain sequences of recombinant prochymosin solubilized from inclusion bodies. J. Protein Chem. 19 277-284.
    • (2000) J. Protein Chem. , vol.19 , pp. 277-284
    • Wei, C.1    Chen, H.2    Zhang, Y.3    Yang, K.4
  • 49
    • 0019494038 scopus 로고
    • Purification and characterization of embryonic chicken pepsinogen, a unique pepsinogen with large molecular weight
    • S. Yasugi and T. Mizuno (1981) Purification and characterization of embryonic chicken pepsinogen, a unique pepsinogen with large molecular weight. J. Biochem. (Tokyo) 89 311-315.
    • (1981) J. Biochem. (Tokyo) , vol.89 , pp. 311-315
    • Yasugi, S.1    Mizuno, T.2
  • 50
    • 84944118073 scopus 로고
    • Chymase
    • E. Abderhalden (Eds), Berlin: J. Springer Verlag
    • E. Zunz (1911) Chymase. E. Abderhalden (Eds) Biochem. Handlexicon 5 Berlin: J. Springer Verlag 618-625.
    • (1911) Biochem. Handlexicon , vol.5 , pp. 618-625
    • Zunz, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.