Fluorescence quenching and time-resolved fluorescence studies of α-mannosidase from aspergillus fischeri (NCIM 508)

Journal of Fluorescence

Volumn 17, Issue 6, 2007, Pages 599-605

  Shashidhara, K S ^a   Gaikwad, Sushama M ^a  

^a NATIONAL CHEMICAL LABORATORY   (India)

Author keywords

Mannosidase; Denaturation; Fluorescence; Lifetime; Solute quenching

Indexed keywords

QUENCHED PROTEINS; SOLUTE QUENCHING; TRYPTOPHANS;

DENATURATION; ENZYMES; ONCOLOGY; QUENCHING;

FLUORESCENCE;

ACRYLAMIDE; ALPHA MANNOSIDASE; CESIUM; CESIUM CHLORIDE; CHLORIDE; N BROMOSUCCINIMIDE; POTASSIUM IODIDE; SUCCINIMIDE; SUCCINIMIDE DERIVATIVE; TRYPTOPHAN;

ARTICLE; ASPERGILLUS; CHEMISTRY; ENZYMOLOGY; ISOLATION AND PURIFICATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; SPECTROFLUOROMETRY;

ACRYLAMIDE; ALPHA-MANNOSIDASE; ASPERGILLUS; BROMOSUCCINIMIDE; CESIUM; CHLORIDES; POTASSIUM IODIDE; PROTEIN CONFORMATION; PROTEIN DENATURATION; SPECTROMETRY, FLUORESCENCE; SUCCINIMIDES; TRYPTOPHAN;

ASPERGILLUS; NEOSARTORYA FISCHERI;

EID: 35949003127     PISSN: 10530509     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10895-007-0227-8     Document Type: Article

References (23)

1. Moremen KW, Trimble R, Herscovics A (1994) Glycosidases of the asparagine-linked oligosaccharide processing pathway. Glycobiology 4:113-125
2. Liao Y-F, Lai A, Moremen KW (1996) Cloning, expression, purification, and characterization of the human broad specificity lysosomal acid α-mannosidase. J Biol Chem 271:28348-28358
3. Neufeld EF (1991) Lysosomal storage diseases. Annu Rev Biochem 60:257-280
4. Henrissat B, Bairoch A (1996) Updating the sequence-based classification of glycosyl hydrolases. Biochem J 316:695-696
5. Goss PE, Baker MA, Carver JP, Dennis JW (1995) Inhibitors of carbohydrate processing: a new class of anticancer agents. Clin Cancer Res 1:935-944
6. Keskar SS, Gaikwad SM, Khan MI (1996) Microbial α-mannosidases. Enzyme Microb Technol 18(8):602-604
7. Eneyskya EV, Kulminskaya AA, Savel'ev AN, Shabalin KA, Golubev AM, Neustroev KN (1998) α-Mannosidase from Trichoderma reesei participates in the postsecretory deglycosylation of glycoproteins. Biochem Biophys Res Commun 245:43-49
8. Kelly SJ, Herscovics A (1998) Glycoprotein biosynthesis in Saccharomyces cerevisiae. Purification of the alpha-mannosidase which removes one specific mannose residue from Man9GlcNAc. J Biol Chem 263:14757-14763
9. Reyna ABV, Noyola PP, Mendez CC, Romero EO, Carreon AF (1999) Purification and biochemical characterization of two soluble alpha-mannosidases from Candida albicans. Glycobiology 9:533-537
10. Mares M, Callewaert N, Piens K, Claeyssens M, Martinet W, Dewalele S, Contreras H, Dewerte I, Penttila M, Contreras R (2000) Molecular cloning and enzymatic characterization of a Trichoderma reesei 1,2-α-d-mannosidase. J Biotechnol 77:255-263
11. 2+-independent 1,2-α-d-mannosidase from Aspergillus saitoi by site-directed mutagenesis. J Biol Chem 278:25289-25294
12. Athanasopoulos VI, Niranjan K, Rastall RA (2005) The production, purification and characterisation of two novel α-d-mannosidases from Aspergillus phoenicis. Carbohydr Res 340:609-617
13. Lehrer SS (1971) Solute perturbation of protein fluorescence. The quenching of tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10:3254-3263
14. Lehrer SS, Leavis PC (1978) Solute quenching of protein fluorescence. Methods Enzymol 49:222-236
15. Lakowicz EM, Weber G (1973) Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry 12:4171-4179
16. Gaikwad SM, Keskar SS, Khan MI (1995) Purification and characterization of α-mannosidase from Aspergillus sp. Biochem Biophys Acta 1250:144-148
17. Gaikwad SM, Khan MI, Keskar SS (1997) Chemical modification of α-mannosidase from Aspergillus sp. Biotechnol Appl Biochem 25:105-108
18. Keskar SS, Gaikwad SM, Khire JM, Khan MI (1993) Production and properties of α-mannosidase from Aspergillus sp. Biotechnol Lett 15:685-690
19. Spande TF, Witkop B (1967) Determination of the tryptophan content of proteins with N-bromosuccinimide. Methods Enzymol 11:498-506
20. Pause E (1978) The chemical modification of tryptophan residues of α-mannosidase from Phaseolus vulgaris. Biochim Biophys Acta 533:446-456
21. Komath SS, Swamy MJ (1999) Fluorescence quenching, time-resolved fluorescence and chemical modification studies on the tryptophan residues of snake gourd (Trichosanthes anguina) seed lectin. J Photochem Photobiol 50:108-118
22. Teale FWJ, Badley RA (1970) Depolarization of the intrinsic and extrinsic fluorescence of pepsinogen and pepsin. Biochem J 116:341-348
23. Sultan NA, Swamy MJ (2005) Fluorescence quenching and time-resolved fluorescence studies on Trichosanthes dioica seed lectin. J Photochem Photobiol B Biol 80:93-100