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2003 | 08 | 2 |

Tytuł artykułu

The use immobilized methylchymotrypsin for the purification of human and sheep alpha-1-proteinase inhibitor [alpha1-PI]

Autorzy

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
α1-proteinase inhibitor was isolated from albumin fractions of human and sheep plasma using a new method of purification using affinity chromatography on immobilized methylchymotrypsin in the presence of 5 M NaCl. The inhibitor was finally polished to homogenity either by chromatography on a Mono Q or a Sephacryl S-200 HR column. The presented method makes it possible to recover α1-proteinase inhibitor which has been added to cow milk.

Wydawca

-

Rocznik

Tom

08

Numer

2

Opis fizyczny

p.363-374,fig.

Twórcy

autor
  • University of Wroclaw, Tamka 2, 50-137 Wroclaw, Poland
autor

Bibliografia

  • 1.Silverman, G.A., Bird, P.I., Carrell, R.W., Church, F.C., Coughlin, P.B., Gettins, P.G.W., Irving, J.A., Lomas, D.A., Luke, C.J., Moyer, R.W., Pemberton, P.A., Remold-O'Donnell, E., Salvesen, G.S., Travis, J. and Whisstock, J.C. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. J. Biol. Chem. 276 (2001) 33293-33296.
  • 2.Hill, R.M., Brennan, S.O. and Birch, N.P. Expression, purification, and functional characterization of the serine protease inhibitor neuroserpin expressed in Drosophila S2 cells. Protein Expr. Purific. 22 (2001) 406-413.
  • 3.Janciauskiene, S. Conformational properties of serine proteinase inhibitors (serpins) confer multiple patophysiological roles. Biochim. Biophys Acta 1535 (2001) 221-235.
  • 4.Mattes, E., Matthiessen, H.P., Turecek, P.L. and Scharz, H.P. Preparation and properties of an alpha-1-protease inhibitor concentrate with high specific activity. Vox Sang 81 (2001) 29-36.
  • 5.Pannell, R., Fohnson, D. and Travis, J. Isolation and properties of human plasma alpha-1-protease inhibitor. Biochemistry 13 (1974) 5439-5445.
  • 6. Glaser, C.B., Chamorro, M., Crowley, R., Karic, L., Childs, A. and Calderon, M. The isolation of alpha-1-proteinase inhibitor by a unique procedure designed for industrial application. Analyt. Biochem. 124 (1982) 364-371.
  • 7. Hein, R.H., van Beveren, S.M., Shearer, M.A., Coan, M.H. and Brockway, W.J. Production of alpha-1-proteinase inhibitor (human). Eur. Respir. J. (Suppl.) 9 (1990) 16-20.
  • 8. Burnouf, T., Constans, J., Clerc, A., Descamps, J., Martinache, L. and Goudemand, M. Biochemical and biological properties of an alpha 1-antitrypsin concentrate. Vox Sang 52 (1987) 291-297.
  • 9. Morihara, K., Tsuzuki, H., Harada, M. and Iwata, T. Purification of human plasma α1-proteinase inhibitor and its inactivation by Pseudomonas aeruginosa elastase. J. Biochem. (Tokyo) 95 (1984) 795-804.
  • 10. Drechsel, D., Karic, L. and Glaser, Ch.B. Affinity chromatography of α1-protease inhibitor using Sepharose-4B-bound anhydrochymotrypsin. Analyt. Biochem. 143 (1984) 141-145.
  • 11.Dubin, A., Potempa, J. and Travis, J. Isolation of nine human plasma proteinase inhibitors by sequential affinity chromatography. Prep. Biochem. 20 (1990) 63-74.
  • 12.Carver, A., Wright, G., Cottom, D., Cooper, J., Dalrymple, M., Temperley, S., Udell, M., Reeves, D., Percy, J., Scott, A., Barrass, D., Gibson, Y., Jeffrey, Y., Samuel, C., Colman, A. and Garner, I. Expression of human alpha 1 antitrypsin in transgenic sheep. Cytotechnology 9 (1992) 77-84.
  • 13.Wilimowska-Pelc, A. and Mejbaum-Katzenellenbogen W. A simple method for isolating trypsin from trichloroacetic acid extracts of bovine pancreas. Anal. Biochem. 90 (1978) 816-820.
  • 14.Nakagawa, Y. and Bender, M.L. Methylation of histidine-57 in α-chymotrypsin by methyl- p-nitrobenzenesulfonate. A new approach to enzyme modification. Biochemistry 9 (1970) 259-267.
  • 15.March, S.C., Parikh, I. and Cuatrescasas, P. A simple method for cyanogen bromide activation of agarose for affinity chromatography. Anal. Biochem. 60 (1974) 149-152.
  • 16.Chase, T. and Shaw, E. Titration of trypsin, plasmin and thrombin with p-nitrophenyl p-guanidinobenzoate HCl. Methods Enzymol. 19 (1970) 20-27.
  • 17.Erlanger, B.F., Kokovsky, N. and Cohen, W. The preparation and properties of two new chromogenic substrates of trypsin . Arch. Biochem. Biophys. 95 (1961) 271-278.
  • 18.Nakajima, K., Powers, J.C., Ashe, B.M. and Zimmerman, M. Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase. Studies with peptide substrates related to the α1-proteinase reactive site. J. Biol. Chem. 254 (1979) 4027-4032.
  • 19.Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254.
  • 20.Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227 (1970) 680-685.
  • 21.Towbin, H., Staehelin, T. and Gordon, J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets. Procedure and some applications. Proc. Natl. Acad. Sci. USA 76 (1979) 4350-4354.
  • 22.Mistry, R., Snashall, P.D., Totty, N., Guz, A. and Tetley, T.D. Isolation and characterization of sheep α1-protease inhibitor. Biochem. J. 273 (1991) 685-690.
  • 23.Wilimowska-Pelc, A., Olichwier, Z., Kowalska, J., Gałuszka, A., Szuszkiewicz, W., Polanowski, A. and Wilusz, T. High concentration of sodium chloride facilitate the use of immobilized chymotrypsin for separating virgin forms of specific trypsin inhibitors. J. Chromatogr. A. 852 (1999) 227-235.
  • 24.Lorenc-Kubis, I., Kowalska, J., Pochroń, B., Żużło, A. and Wilusz, T. Isolation and amino acid sequence of a serine proteinase inhibitor from common flax (Linum usitatissimum) seeds. Chembiochem. 2 (2001) 45-51.
  • 25.Leluk, J., Otlewski, J., Wieczorek, M., Polanowski, A. and Wilusz, T. Preparation and characteristics of trypsin inhibitors from the seeds of squash (Cucurbita maxima) and zuzchini (Cucurbita pepo var. giromontia). Acta Biochim. Polon. 30 (1983) 127-138.
  • 26.Ako, H., Foster, R.J. and Ryan, C.A. The preparation of anhydro-trypsin and its reactivity with naturally occuring proteinase inhibitors. Biochim. Biophys. Res. Commun. 47 (1972) 1402-1407.

Typ dokumentu

Bibliografia

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