PL EN


Preferences help
enabled [disable] Abstract
Number of results
2003 | 50 | 3 | 765-773
Article title

Non-conventional affinity chromatography of serine proteinases and their inhibitors.

Content
Title variants
Languages of publication
EN
Abstracts
EN
From among a wide variety of protein purification techniques affinity chromatography has proved to be particularly effective for separation of proteolytic enzymes and their inhibitors. In this article, following a general description of affinity adsorbents used for purification of proteinases, we overview a simple separation procedure for some serine proteinases and their inhibitors by way of affinity chromatography in the presence of high NaCl concentration. It has been shown that some highly specific trypsin inhibitors exhibit also antichymotrypsin activity when high concentration of Na+ but not K+ or Li+ ions are present in the reaction mixture. Taking advantage of this phenomenon the virgin forms of trypsin inhibitors from squash seeds, Kazal-type inhibitor from porcine pancreas and α1-proteinase inhibitor from human and sheep plasma, as an example, were separated using immobilized chymotrypsin or its inactive derivative methylchymotrypsin in the presence of 5 M NaCl.
Year
Volume
50
Issue
3
Pages
765-773
Physical description
Dates
published
2003
received
2003-05-30
revised
2003-08-23
accepted
2003-09-04
References
  • Ako H, Foster RJ, Ryan CA. (1972) The preparation of anhydro-trypsin and its reactivity with naturally occurring proteinase inhibitors. Biochem Biophys Res Commun.; 47: 1402-7.
  • Anvar A, Saleemuddin M. (2002) Purification and characterization of digestive alkaline protease from the larvae of Spilosoma obliqua. Archiv Insect Biochem Physiol.; 51: 1-12.
  • Basak A, Gong YT, Cromlish JA, Paquin JA, Jean F, Seidah NG, Lazure C, Chretien M. (1990) Syntheses of argininal semicarbazone containing peptides and their application in the affinity chromatography of serine proteinases. Int J Pept Protein Res.; 36: 7-17.
  • Baugh RJ, Travis J. (1976) Human leukocyte granule elastase: Rapid isolation and characterization. Biochemistry.; 15: 836-41.
  • Bogard WC. Jr, Laskowski M Jr. (1979) Turkey pancreatic secretory trypsin inhibitor. Federation of American Societies for Experimental Biology, 63rd. Annual Meeting, Abstracts of papers; 836, Abstract 3193.
  • Cuatrecasas P, Wilchek M, Anfinsen CB. (1968) Selective enzyme purification by affinity chromatography. Proc Natl Acad Sci U S A.; 61: 636-43.
  • Drechsel D, Karic L, Glaser CB. (1984) Affinity chromatography of α1-protease inhibitor using Sepharose-4B-bound anhydrochymotrypsin. Anal Biochem.; 143: 141-5.
  • Eijsink VGH, van den Burg B, Venema G. (1991) High performance affinity chromatography of Bacillus neutral proteases. Biotechnol Appl Biochem.; 14: 275-83.
  • Feinstein G. (1970) Purification of trypsin by affinity chromatography on ovomucoid-Sepharose resin. FEBS Lett.; 7: 353-5.
  • Fritz H, Schult H, Hutzel M, Wiedemann M, Werle E. (1967) On protease inhibitors. IV. Isolation of protease inhibitors with the aid of water insoluble enzyme resins. Hoppe Seylers Z Physiol Chem.; 348: 308-12.
  • Gonciarz M. (1996) Site directed mutagenesis of CMTI I inhibitor from the seeds of Cucurbitaceae plants. The influence of NaCl on energy of interactions between serine proteinases and protein inhibitors. MSc Thesis, University of Wrocław, (in Polish).
  • Grybel J, Wilusz T. (2003) The use of immobilized methylchymotrypsin for the purification of human and sheep alpha-1-proteinase inhibitor (α1PI). Cell Mol Biol Lett.; 8: 363-74.
  • Guyonnet V, Tłuscik F, Long PL, Polanowski A, Travis J. (1999) Purification and partial characterization of the pancreatic proteolytic enzymes trypsin, chymotrypsin, and elastase from the chicken. J Chromatogr A.; 852: 217-25.
  • Irvine JW, Coombs GH, North MJ. (1993) Purification of cysteine proteinases from trichomonads using bacitracin-Sepharose. FEMS Microbiol Lett.; 110: 113-9.
  • Ishi S, Kasai K. (1980) Affinity methods using arginine derivatives. Methods Enzymol.; 80: 842-8.
  • Jakimowicz P. (1996) The effect of salt, methanol and saccharose on the interaction of selected proteinases with substrates and protein inhibitors. MSc thesis, University of Wrocław, (in Polish).
  • Kanamori A, Seno N, Matsumoto I. (1986) Preparation of high-capacity affinity adsorbents using formyl carriers and their use for low- and high-performance liquid affinity chromatography of trypsin-family proteases. J Chromatogr.; 363: 231-42.
  • Kassell B, Marciniszyn MB. (1971) A simple method of purification of the basic trypsin inhibitor of bovine organs. In Proceedings of the International Research Conference on Proteinase Inhibitors. Fritz H, Tschesche H. eds, pp 43-46. Walter de Gruyter, Berlin, New York.
  • Kobayashi H, Murakami K. (1978) Rapid and large scale isolation of chymosin (rennin) by pepstatin-aminohexylagarose. Agric Biol Chem.; 42: 2227-31.
  • Kowalska J. (2002) A new method of separation of serine proteinase inhibitors from the seeds of Cyctanthera pedata, Linum usitatissimum and Cannabis sativa. PhD Thesis, University of Wrocław, (in Polish).
  • Kučerovä Z, Pohl J, Korbovä L. (1986) Separation of human pepsin and gastricsin by affinity chromatography with an immobilized synthetic inhibitor. J Chromatogr.; 376: 409-12.
  • Laskowski M Sr, Schneider SL, Wilson KA, Kress LF, Mozejko JH, Martin SR, Kucich U, Andrews M. (1971) Naturally occurring trypsin inhibitors: further studies on purification and temporary inhibition. In Proceedings of the International Research Conference on Proteinase Inhibitors. Fritz H, Tschesche H. eds, pp 66-73. Walter de Gruyter, Berlin, New York.
  • Leung D, Abbenante G, Fairlie DP. (2000) Proteinase inhibitors: current status and future prospects. J Med. Chem.; 43: 305-41.
  • Liau DF, Yin NX, Ryan SF. (1993) Isolation of human polymorphonuclear leukocyte elastase by chromatography on immobilized benzamidine. Prep Biochem.; 23: 439-47.
  • Lorenc-Kubis I, Kowalska J, Pochroń B, Żużlo A, Wilusz T. (2001) Isolation and amino acid sequence of a serine proteinase inhibitor from common flax (Linum usitatissimum) seeds. Chembiochem.; 2: 45-51.
  • Makriyannis T, Clonis YD. (1997) Design and study of peptide-ligand affinity chromatography adsorbents: application to the case of trypsin purification from bovine pancreas. Biotech Bioeng.; 53: 49-57.
  • Polanowski A, Wilusz T, Nienartowicz B, Cieślar E, Slomińska A, Nowak K. (1980) Isolation and partial amino acid sequence of the trypsin inhibitors from the seeds of Cucurbita maxima. Acta Biochim Polon.; 27: 371-82.
  • Polanowski A, Cieślar E, Otlewski J, Nienartowicz B, Wilimowska-Pelc A, Wilusz T. (1987) Protein inhibitors of trypsin from the seeds of Cucurbitaceae plants. Acta Biochim Polon.; 34: 395-406.
  • Robinson NC, Tye RW, Neurath H, Walsh KA. (1971) Isolation of trypsins by affinity chromatography. Biochemistry.; 10: 2743-7.
  • Rudenskaya GN, Bogdanova EA, Revina LP, Golovkin BN, Stepanov VM. (1995) Macluralisin - a serine proteinase from fruits of Maclura pomifera (Raf.) Schneid. Planta.; 196: 174-9.
  • Ryan DS, Feeney RE. (1975) The interaction of inhibitors of proteolytic enzymes with 3-methylhistidine-57-chymotrypsin. J Biol Chem.; 250: 843-7.
  • Thompson AR, Davie EW. (1971) Affinity chromatography of thrombin. Biochim Biophys Acta.; 250: 210-5.
  • Tombaccini D, Mocali A, Weber E, Paoletti F. (2001) A cystatin-based affinity procedure for the isolation and analysis of papain-like cysteine proteinases from tissue extracts. Anal Biochem.; 289: 231-8.
  • Turk V, Uhr I, Kregar J, Babnik F, Gubensek F, Smith R. (1977) Purification and some properties of native and immobilized cathepsinD. In Intracellular Protein Catabolism II. Turk V, Marks N. eds, pp 240-9. Plenum Press, New York, London.
  • Wątorek W, Polanowski A, Wilusz T. (1996) The use of sequential affinity chromatography for separation of human neutrophil elastase, cathepsin G and azurocidin. Acta Biochim Polon.; 43: 503-6.
  • Wesołowska O, Krokoszyńska I, Krowarsch D, Otlewski J. (2001) Enhancement of chymotrypsin-inhibitor/substrate interactions by 3 M NaCl. Biochim Biophys Acta.; 1545: 78-85.
  • Wilimowska-Pelc A, Polanowski A, Kołaczkowska MK, Wieczorek M, Wilusz T. (1983a) Aspartyl proteinase from cucumber (Cucumis sativus) seeds. Preparation and characteristics. Acta Biochim Polon.; 30: 23-31.
  • Wilimowska-Pelc A, Wieczorek M, Otlewski J, Leluk J, Wilusz T. (1983b) Immobilized Bowman-Birk inhibitor for selective isolation of chymotrypsin B from bovine pancreas. J Chromatogr.; 269: 22-7.
  • Wilimowska-Pelc A, Stachowiak D, Gładysz M, Olichwier Z, Polanowski A. (1996) Antiproteolytic activity of goose pancreas: purification, inhibitory properties and amino acid sequence of a Kazal type trypsin inhibitor. Acta Biochim Polon.; 43: 489-96.
  • Wilimowska-Pelc A, Olczak M, Olichwier Z, Gładysz M, Wilusz T. (1999a) Isolation and amino acid sequence of two trypsin isoinhibitors from duck pancreas. Comp Biochem Physiol B Biochem Mol Biol.; 124: 281-8.
  • Wilimowska-Pelc A, Olichwier Z, Kowalska J, Gałuszka A, Szuszkiewicz W, Polanowski A, Wilusz T. (1999b) High concentrations of sodium chloride facilitate the use of immobilized chymotrypsin for separating virgin forms of specific trypsin inhibitors. J Chromatogr A.; 852: 227-35.
  • Wilusz T, Polanowski A. (1985) Pepstatin-sensitive proteinase from Chlamydomonas reinhardtii. In Aspartic Proteinases and their Inhibitors. Kostka V. ed, pp 45-48. Walter de Gruyter & Co, Berlin, New York.
  • Żelazko M. (2000) Isolation of proteolytic enzymes from goose pancreases with affinity chromatography on immobilized inhibitors. MSc Thesis, University of Wroclaw, (in Polish).
Document Type
Publication order reference
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv50i3p765kz
Identifiers
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.