1Zhang Y, Proenca R, Maffei M, et al. Positional cloning of the mouse obese gene and its human homologue [ J]. Nature, 1994,372: 425-432.
2Cohen S L, Halaas J L, Friedman J M, et al. Human leptin characterization [J]. Nature, 1996,382:589-199.
3Gong D W, Bi S, Pratley R E, et al. Genomic structure and promoter analysis of the human obese gene [J]. Bio. Chem, 1995,27 (8) : 3971-3974.
4Peneymounter M A, Cullen M J, Baker M B, et al. Effects of the obese gene product on body weight regulation in ob/ob mice [J]. Science, 1995,269:540-543.
6Zhang F, Basinski M B. Crystal structure of the obese protein leptin-E 100 [J]. Nature, 1997,387:206-209.
7Johnson R M, Johnson T M, Londraville R L. Evidence for leptin expression in fishes [J]. J Exp Zool, 2000,286(7) :718-724.
8Yaghoubian S, Filosa M F, Youson J H . Proteins immunoreactive with antibody against a human leptin fragment are found in serum and tissues of the sealamprey, Petromyzon marinus L. [ J] . Comp BiochemPhysiol B Biochem Mol Biol., 2001,129(4):777-785.
4Zhao K H,Scheer H. Type Ⅰ and type Ⅱ reversible photochemistry of phycoerythrocyanin α-subunit from Mastigocladus Laminosus both involve Z,E isomerization of phycoviolobilin chromophore and are controlled by sulfhydryls in apoprotein [J].Biochimica et Biophysica Acta. 1995,1228:244
5Zhao K H.Rainer Haessner, Edmund Cmiel, Hugo Scheer, Type I reversible photochemistry of phycoerythrocyanin involves Z/E-isomerization of α-84 phycoviolobilin chromophore[J].Biochemica et Biophysica Acta.1995,1228:235
6Sambrook J, Fritsch E F,Maniatis T.Molecular Cloning A laboratory manual (second. ed.)[M].New York:Cold Spring Harbor Laboratory Press,1989
7Studier F W,Moffatt P A. Analysis of bacteriophage T7 early RNAs and proteins on slab gels [J].J.Mol. Biol.,1986,189:113
8O′Carra, P. and O′hEocha, C. Bilins released from algae and bilinproteins by methanolic extraction.[J].Phytochemistry 5,1966,993
9Ebelein M, Kufer W.Genes encoding both subunits of phycoerythrocyanin, a light-harvesting biliprotein from the cyanobacterium Mastigocladus laminosus[J].Gene,1990,94:133
1Hibbetts k,Hines B,Williams D.An overview of proteinase inhibitors[J].Journal of Veterinary Internal Medicine,1999,13(4):302-308.
2Laskowski M,Kato I.Protein inhibitors of proteinases[J].Annual Review of Biochemistry,1980,49:593-626.
3Krowarsch D,Cierpicki T,Jelen F,et al.Canonical protein inhibitors of serine proteases[J].Cellular and Molecular Life Sciences,2003,60:2427-2444.
4Irving J,Pike R Lesk A,et al.Phylogeny of the serpin su-perfamily:Implications of patterns of amino acid conserva-fion for structure and function[J].Genome Research,2000,10:1845-1864.
5Silverman G,Bird P,Carrell R,et al.The Serpins are an expanding superfamily of structurally similar but function-ally diverse proteins[J].Journal of Biological Chemistry,2001.276(36):293-296.
6Duellman W E,Trueb L.Biology of Amphibians[M].New York:McGraw-Hill Book Company,1986,670.
7Bevins C L,Zasloff M.Peptides from frog skin[J].Annual Review of Biochemistry,1990,59:395-414.
8Mignogna G,Pasearella S,Wechselberger C,et al.BSTI,a trypsin inhibitor from skin secretions of Bombina bombina related to protease inhibitors of nematodes[J].Protein Science,1996,5:357-362.
9Lai R,Liu H,Lee WH,et al.Identification and cloning of a trypsin inhibitor from skin secretions of Chinese red-belly toad Bombina maxima[J].Comparative Biochemistry and Physiology B:Biochemistry and Molecular Biology,2002,131:47-53.
10Conlon J M,Kim J B.Protease inhibitor of the Kunitz family from skin secretions of the tomato frog,Dyscophus guineti[J].Biochemical and Biophysical Research Communications.2000.279(3):961-964.