Calcium-binding and structural stability of echidna and canine milk lysozymes

Protein Science

Volumn 7, Issue 10, 1998, Pages 2150-2155

  Kikuchi, Masayuki ^a   Kawano, Keiichi ^a   Nitta, Katsutoshi ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

Author keywords

Calcium binding; Canine; Equine; Lysozyme; Molecular evolution; Molten globule

Indexed keywords

ALPHA LACTALBUMIN; LYSOZYME;

AMINO ACID SEQUENCE; ARTICLE; CALCIUM BINDING; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; DOG; ECHIDNA; ENZYME STABILITY; MILK; MOLECULAR EVOLUTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING;

ANIMALIA; AVES; CANIS FAMILIARIS; COLUMBA; EQUIDAE; EUTHERIA;

EID: 0031789584     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560071012     Document Type: Article

References (27)

1. Acharya KR, Stuart DI, Walker NPC, Lewis M, Phillips DC. 1989. Refined structure of baboon α-lactalbumin at 1.7A resolution: Comparison with C-type lysozyme. J Mol Biol 208:99-127.
2. Anderson PJ, Brooks CL, Berliner LJ. 1997. Functional identification of calcium binding residues in bovine α-lactalbumin. Biochemistry 36:11648-11654.
3. Brew K, Castellino FJ, Vanaman TC, Hill RL. 1970. The complete amino acid sequence of bovine α-lactalbumin. J Biol Chem 245:4570-4582.
4. 2+ to bovine α-lactalbumin and equine lysozyme. J Inorg Biochem 37:185-191.
5. Grobler JA, Rao KR, Pervaiz S, Brew K. 1994. Sequences of two highly divergent canine type c lysozymes: Implications of the evolutionary origins of the lysozyme/α-lactalbumin superfamily. Arch Biochem Biophys 313:360-366.
6. Guss JM, Messer M, Costello M, Hardy K, Kumar V. 1997. The structure of the calcium-binding echidna milk lysozyme at 1.9A resolution. Acta Crystallographica D53:355-363.
7. 2+-binding site into human lysozyme. Protein Eng 6:643-649.
8. Hiraoka Y, Segawa T, Kuwajima K, Sugai S, Murai N. 1980. α-Lactalbumin: A calcium metalloprotein. Biochem Biophys Res Commun 95:1098-1104.
9. Hiraoka Y, Sugai S. 1985. Equilibrium and kinetic study of sodium-and potassium-induced conformational changes of apo-α-lactalbumin. Int J Peptide Protein Res 26:252-261.
10. Kita N, Kuwajima K, Nitta K, Sugai S 1976. Equilibrium and kinetics of the unfolding of α-lactalbumin by guanidine hydrochloride(II). Biochim Biophys Acta 427:350-358.
11. Kuwajima K, Hiraoka Y, Ikeguchi M, Sugai S. 1985. Comparison of the transient folding intermediates in lysozyme and α-lactalbumin. Biochemistry 24:874-881.
12. Kuwajima K, Nitta K, Yoneyama M, Sugai S. 1976. Three-state denaturation of a-lactalbumin by guanidine hydrochloride. J Mol Biol 106:359-373.
13. Morozova-Roche LA, Arico-Muendel CC, Haynie DT, Emelyanenko VI, Van Dael H, Dobson CM. 1997. Structural characterization and comparison of the native and A-states of equine lysozyme. J Mol Biol 268:903-921.
14. Nitta K, Sugai S. 1989. The evolution of lysozyme and α-lactalbumin. Eur J Biochem 182:111-118.
15. Nitta K, Tsuge H, Iwamoto H. 1993. A comparative study of the stability of the folding intermediates of the calcium-binding lysozymes. Int J Peptide Protein Res 41:118-123.
16. Nitta K, Tsuge H, Shimazaki K, Sugai S. 1988. Calcium-binding lysozymes. Biol Chem Hoppe-Seyler 369:671-675.
17. Nitta K, Tsuge H, Sugai S, Simazaki K. 1987. The calcium-binding property of equine lysozyme. FEBS Lett 223:405-408.
18. Nozaka M, Kuwajima K, Nitta K, Sugai S. 1978. Detection and characterization of the intermediate on the folding pathway of human α-lactalbumin. Biochemistry 17:3753-3758.
19. Pervaiz S, Brew K. 1986. Purification and characterization of the major whey proteins from the milks of the bottle nose dolphin (Tursiops truncatus), the Florida manatee (Trichechus manatus latirostris), and the beagle (Canis familiaris). Arch Biochem Biophys 246:864-854.
20. Pike ACW, Brew K, Acharya KR. 1996. Crystal structures of guinea pig, goat and bovine α-lactalbumins highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase. Structure 4:691-703.
21. Prager EM, Jolles P. 1996. Animal lysozymes c and g: An overview. In: Jolles P, ed. Lysozymes: Model enzymes in biochemistry and biology. Basel-Boston-Berlin: Birkhauzer Verlag. pp 9-31.
22. Qasba PK, Safaya SK. 1984. Similarity of the nucleotide sequences of rat α-lactalbumin and chicken lysozyme genes. Nature 308:377-380.
23. Stuart DI, Acharya KR, Walker NPC, Smith SG, Lewis M, Phillips DC. 1986. α-Lactalbumin possesses a novel calcium binding loop. Nature 324:84-87.
24. Teahan CG, Mackenzie HA, Shaw DC, Griffiths M. 1991. The isolation and amino acid sequences of echidna (Tachyglossus aculeatus) milk lysozyme I and II. Biochem Int 24:85-95.
25. 1H NMR. Biochim Biophys Acta 1078: 77-84.
26. Van Dael H, Haezebrouck P, Morozova L, Arico-Muendel C, Dobson CM. 1993. Partially folded states of equine lysozyme. Structural characterization and significance for protein folding. Biochemistry 32:11886-11894.
27. Wetlaufer DB. 1962. Ultraviolet spectra of proteins and amino acids. Adv Protein Chem 17:303-390.