PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2007 | 63 | 03 |

Tytuł artykułu

Inhibitory trypsyny z rodziny Bowmana-Birka - budowa oraz znaczenie w zywieniu ludzi i zwierzat

Warianty tytułu

EN
Bowman-Birk trypsin inhibitors: their structure and value in human and animal feeding

Języki publikacji

PL

Abstrakty

EN
Bowman-Birk inhibitors (BBI) are small serine proteinase inhibitors found in the leguminous and gramineous plants. Characteristically, their molecular masses are in the range of 6-9 kDa and are rich in disulfide bonds. The name of this family comes from the names of workers who first isolated (Bowman, 1940) and characterized (Birk, 1961) this inhibitor from soybean. Soybean BBI is the best known inhibitor of this family and it is often called ‘classical BBI’. The Bowman-Birk inhibitor is recognized as a potential cancer chemopreventive agent for humans. Human populations consuming large amounts of BBI in their diet have been demonstrated to exhibit lower rates of colon, breast, prostate and skin cancers.

Wydawca

-

Rocznik

Tom

63

Numer

03

Opis fizyczny

s.276-281,rys.,tab.,bibliogr.

Twórcy

  • Akademia Rolnicza, ul.Akademicka 13, 20-634 Lublin

Bibliografia

  • 1.Asao T., Imai F., Tsuji I., Tashiro M., Iwami K., Ibuki F.: The amino acid sequence of a Bowman-Birk type proteinase inhibitor from faba beans (Vicia faba L.). J. Biochem. 1991, 110, 951-955.
  • 2.Armstrong W. B., Kennedy A. R., Wan X. S., Atiba J., McLaren Ch. E., Meyskens Jr. F. L.: Single-dose administration of Bowman-Birk inhibitor concentrate in patients with oral leukoplakia. Cancer Epidemiol. Biom. Prev. 2000, 9, 43-47.
  • 3.Boateng J. A., Viquez O. M., Konan K. N., Dodo H. W.: Screening of a peanut (Arachis hypogaea L.) cDNA library to isolate a Bowman-Birk trypsin inhibitor clone. J. Agric. Food Chem. 2005, 53, 2028-2031.
  • 4.Brown W. E., Takio K., Titani K., Ryan C. A.: Wound-induced trypsin inhibitor in alfalfa leaves: identity as a member of the Bowman-Birk inhibitor family. Biochem. 1985, 24, 2105-2108.
  • 5.Catalano M., Ragona L., Molinari H., Tava A., Zetta L.: Anticarcinogenic Bowman Birk inhibitor isolated from snail medic seeds (Medicago scutellata): solution structure and analysis of self-association behavior. Biochemistry 2003, 42, 10, 2836-2846.
  • 6.Chen Y. W., Huang S. Ch., Lin-Shiau S. Y., Lin J. K.: Bowman Birk inhibitor abates proteasome function and suppresses the proliferation of MCF7 breast cancer cells through accumulation of MAP kinase phosphatase-1. Carcinogenesis 2005, 26, 1296-1306.
  • 7.Clemente A., Gee J. M., Johnson I. T., Mackenzie D. A., Domoney C.: Pea (Pisum sativum L.) protease inhibitors from the Bowman-Birk class influence the growth of human colorectal adenocarcinoma HT29 cells in vitro. J. Agric. Food Chem. 2005, 53, 8979-8986.
  • 8.Deshimaru M., Watanabe A., Suematsu K., Hatano M., Terada S.: Purification, amino s, and cDNAc of trypsin inhibitors from onion (Allium cepa L.) bulbs. Biosci. Biotechnol. Biochem. 2003, 67, 1653-1659.
  • 9.Deshimaru M., Yoshimi S., Shioi S., Terada S.: Multigene family for Bowman-Birk type proteinase inhibitors of wild soya and soybean: the presence of two BBI-a genes and pseudogenes. Biosci. Biotechnol. Biochem. 2004, 68, 1279-1286.
  • 10.Ferrasson E., Quillien L., Gueguen J.: Amino acid sequence of a Bowman-Birk proteinase inhibitor from pea seeds. J. Protein Chem. 1995, 14, 6, 467-475.
  • 11.Grela E. R., Winiarska A.: Influence of different conditions of extrusion on the antinutritional factors content in grass pea (Lathyrus sativus L.) seeds. Proc. 3rd Europ. Conf. Grain Legumes. Walladdid, Spain 1998, 2, 101-102.
  • 12.Hammond R. W., Foard D. E., Larkins B. A.: Molecular cloning and analysis of a gene coding for the Bowman-Birk protease inhibitor in soybean. J. Biol. Chem. 1984, 259, 9883-9890.
  • 13.Iingling L., Jianjun L., Song-Ming, Liyun L., Bihao C.: Study on transformation of cowpea trypsin inhibitor gene into cauliflower (Brassica oleracea L. var. botrytis). Afr. J. Biotechnol. 2005, 4, 45-49.
  • 14.Kaankuka F. G., Balogun T. F., Tegbe T. S. B.: Effects of duration of cooking of full-fat soya beans on proximate analysis, levels of antinutritional factors, and digestibility by weanling pigs. Ann. Feed. Sci. Technol. 1996, 62, 229-237.
  • 15.Kennedy A. R., Billings P. C., Wan X. S., Newberne P. M.: Effects of Bowman-Birk inhibitor on rat colon carcinogenesis. Nutr. Canc. 2002, 43, 174-186.
  • 16.Khalil A. A.: Nutritional improvement of an Egyptian breed of mung bean by probiotic lactobacilli. Afr. J. Biotechnol. 2006, 5, 206-212.
  • 17.Kimura M., Kouzuma Y., Abe K., Yamasaki N.: On a Bowman-Birk family proteinase inhibitor from Erythrina variegata seeds. J .Biochem. (Tokyo) 1994, 115, 369-372.
  • 18.Kulasek G., Leontowicz H., Krzemiński R.: Bioaktywne substancje w pokarmach dla ludzi i zwierząt (cz. I). Czynniki antyżywieniowe. Mag. Wet. 1995, 15, 39-44.
  • 19.Kumar P., Rao A. G. A., Hariharaputran S., Chandra N., Gowda L. R.: Molecular mechanism of dimerization of Bowman-Birk inhibitors. J. Biol. Chem. 2004, 279, 30425-30432.
  • 20.McGurl B., Mukherjee S. K., Kahn M. L., Ryan C. A.: Cloning and characterization of two Bowman-Birk proteinase inhibitors from alfalfa (Medicago sativa var. Vernema). Plant Mol. Biol. 1995, 27, 995-1001.
  • 21.Mosolov V. V., Valueva T. A.: Proteinase inhibitors and their function in plants: a review. Applied Biochem. Microbiol. 2005, 41, 261-282.
  • 22.Mulvenna J. P., Foley Fi. M., Craik D. J.: Discovery, structural determination, and putative processing of the precursor protein that produces the cyclic trypsin inhibitor sunflower trypsin inhibitor 1. J. Biol. Chem. 2005, 280, 32245-32253.
  • 23.Ng T. B., Lam S. K., Fong W. P.: A homodimeric sporamin-type trypsin inhibitor with antiproliferative, HIV reverse transcriptase-inhibitory and antifungal activities from wampee (Clausena lansium) seeds. Biol. Chem. 2003, 384, 289-293.
  • 24.Odani S., Ikenaka T.: Studies on soybean trypsin inhibitors. XI. Complete amino acid sequence of a soybean trypsin-chymotrypsin-elastase inhibitor, C-II. J. Biochem. (Tokyo) 1977a, 82, 1523-1531.
  • 25.Odani S., Ikenaka T.: Studies on soybean trypsin inhibitors. X. Isolation and partial characterization of four soybean double-headed proteinase inhibitors. J. Biochem. (Tokyo) 1977b, 82, 1513-1522.
  • 26.Qu L.-J., Chen J., Liu M., Pan N., Okamoto H., Lin Z., Li Ch., Li D., Wang J., Zhu G., Zhao X., Chen X., Gu H., Chen Z.: Molecular cloning and functional analysis of a novel type of Bowman-Birk inhibitor gene family in rice. Plant Physiol. 2003, 133, 560-570.
  • 27.Raj. S. S., Kibushi E., Kurasawa T., Suzuki A., Yamane T., Odani S., Iwasaki Y., Yamane T., Ashida T.: Crystal structure of bovine trypsin and wheat germ trypsin inhibitor (I-2b) complex (2:1) at 2.3 a resolution. J. Biochem. 2002, 132, 927-933.
  • 28.Roy D. M., Schneeman B. O.: Effect of soy protein, casein and trypsin inhibitor on cholesterol, bile acids and pancreatic enzymes in mice. J. Nutr. 1981, 111, 878-885.
  • 29.Song H. K., Kim Y. S., Yang J. K., Moon J., Lee J. Y., Suh S. W.: Crystal structure of a 16 kDa double-headed Bowman-Birk trypsin inhibitor from barley seeds at 1.9 A resolution. J. Mol. Biol. 1999, 293, 1133-1144.
  • 30.Su G., Chang K. C.: Trypsin inhibitor activity in vitro digestibility and sensory quality of meat-like yuba products as affected by processing. J. Food Sci. 2002, 67, 1260-1266.
  • 31.Suzuki A., Kurasawa T., Tashiro C., Hasegawa K., Yamane T., Ashida T., Odani S.: Crystallization and preliminary X-ray studies on the trypsin inhibitor I-2 from wheat germ and its complex with trypsin. Acta Cryst. 1993, 49, 594-596.
  • 32.Tashiro M., Hashino K., Shiozaki M., Ibuki F., Maki Z.: The complete amino acid sequence of rice bran trypsin inhibitor. J. Biochem. (Tokyo) 1987, 102, 297-306.
  • 33.Tashiro M., Maki Z.: Purification and characterization of a trypsin inhibitor from rice bran. J. Nutr. Sci. Vitaminol. (Tokyo) 1979, 25, 255-264.
  • 34.Valueva T. A., Mosolov V. V.: Role of inhibitors of proteolytic enzymes in plant defense against phytopathogenic microorganisms. Biochem. (Moscow) 2004, 69, 1305-1309.
  • 35.Weder J. K., Hinkers S. C.: Complete amino acid sequence of the lentil trypsin-chymotrypsin inhibitor LCI-1.7 and a discussion of atypical binding sites of Bowman-Birk inhibitors. J. Agric. Food Chem. 2004, 52, 4219-4226.
  • 36.Weder J. K., Kahleyss R.: Isolation and characterisation of four trypsin-chymotrypsin inhibitors from lentil seeds. J. Sci. Food Agric. 1998, 78, 429-434.
  • 37.Whiting A. K., Peticolas W. L.: Details of the acyl-enzyme intermediate and the oxyanion hole in serine protease catalysis. Biochem. 1994, 33, 552-561.
  • 38.Witschi H., Kennedy A. R.: Modulation of lung tumor development in mice with the soybean-derived Bowman-Birk protease inhibitor. Carcinogenesis 1989, 10, 2275-2277.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-becf174c-6c2f-48ae-b203-77eb711f2470
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.