View Item 

Show simple item record

The lectin from leaves of Japanese cycad, Cycas revoluta Thunb. (gymnosperm) is a member of the jacalin-related family
dc.contributor.authorYagi, Fumioen_US
dc.contributor.authorIwaya, Toshinobuen_US
dc.contributor.authorHaraguchi, Tomokazuen_US
dc.contributor.authorGoldstein, Irwin J.en_US
dc.date.accessioned2010-04-01T15:09:27Z
dc.date.available2010-04-01T15:09:27Z
dc.date.issued2002-09en_US
dc.identifier.citationYagi, Fumio; Iwaya, Toshinobu; Haraguchi, Tomokazu; Goldstein, Irwin J. (2002). "The lectin from leaves of Japanese cycad, Cycas revoluta Thunb. (gymnosperm) is a member of the jacalin-related family." European Journal of Biochemistry 269(17): 4335-4341. <http://hdl.handle.net/2027.42/65624>en_US
dc.identifier.issn0014-2956en_US
dc.identifier.issn1432-1033en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/65624
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=12199712&dopt=citationen_US
dc.format.extent429095 bytes
dc.format.extent3110 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherBlackwell Science Ltden_US
dc.rightsFEBS, 2002en_US
dc.subject.otherCycas Revoluta Thunb.en_US
dc.subject.otherGymnospermen_US
dc.subject.otherJapanese Cycaden_US
dc.subject.otherLeafen_US
dc.subject.otherLectinen_US
dc.titleThe lectin from leaves of Japanese cycad, Cycas revoluta Thunb. (gymnosperm) is a member of the jacalin-related familyen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry, Medical School, The University of Michigan, Ann Arbor, Michigan, USAen_US
dc.contributor.affiliationotherDepartment of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, Kagoshima, Japan;en_US
dc.identifier.pmid12199712en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/65624/1/j.1432-1033.2002.03127.x.pdf
dc.identifier.doi10.1046/j.1432-1033.2002.03127.xen_US
dc.identifier.sourceEuropean Journal of Biochemistryen_US
dc.identifier.citedreferenceEtzler, M. E. ( 1986 ) Distribution and function of plant lectins. In The Lectins ( Liener, I. E. & Sharon, N. & Goldstein, I. J., eds), pp. 371 – 435. Academic Press Inc., Orlando FL.en_US
dc.identifier.citedreferenceStrosberg, A. D., Buffard, D., Lauwereys, M. & Foriers, A. ( 1986 ) Legume lectins: a large family of homologous proteins. In The Lectins ( Liener, I. E. & Sharon, N. & Goldstein, I. J., eds), pp. 249 – 264. Academic Press Inc., Orlando FL.en_US
dc.identifier.citedreferenceLis, H. & Sharon, N. ( 1986 ) Application of lectins. In The Lectins ( Liener, I. E. & Sharon, N. & Goldstein, I. J., eds), pp. 293 – 370. Academic Press Inc, Orlando FL.en_US
dc.identifier.citedreferenceVan Damme, E. M. J., Peumans, W. J., Barre, A. & Rouge, P. ( 1998 ) Plant lectins: a composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles. Crit. Rev. Plant Sci. 17, 575 – 692.en_US
dc.identifier.citedreferenceDatta, P. K., Figueroa, M. O. D. C. R. & Lajolo, F. M. ( 1991 ) Purification and characterization of two major lectins from Araucaria brasiliensis syn. Araucaria angustifolia Seeds (Penh). Plant Physiol. 97, 856 – 862.en_US
dc.identifier.citedreferencePettitt, J. M. ( 1977 ) Detection in primitive gymnospermsof proteins and glycoproteins of possible significance in reproduction. Nature 266, 530 – 532.en_US
dc.identifier.citedreferenceLowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. ( 1951 ) Protein measurement with the folin phenol reagent. J. Biol. Chem. 193, 265 – 275.en_US
dc.identifier.citedreferenceDubois, M., Gilles, K. A., Hamilton, H. K., Rebers, P. A. & Smith, F. ( 1956 ) Colorimetric method for determination of sugars and related substances. Anal. Chem. 28, 350 – 356.en_US
dc.identifier.citedreferenceDavis, B. J. ( 1964 ) Disc electrophoresis II, methods and application to human serum proteins. Ann. NY Acad. Sci. 121, 404 – 427.en_US
dc.identifier.citedreference 10.  Laemmli, U.K. ( 1970 ) Cleavage of structural proteins during theassembly of the head of bacteriophage T4. Nature 227, 680 – 685.en_US
dc.identifier.citedreferenceHirs, C. H. W. ( 1956 ) The oxidation of ribonuclease with performic acid. J. Biol. Chem. 219, 611 – 621.en_US
dc.identifier.citedreferenceSo, L. L. & Goldstein, I. J. ( 1967 ) Protein–carbohydrate interaction VI. Application of the quantitative precipitin method to polysaccharide–concanavalin A interaction. J. Biol. Chem. 242, 1617 – 1622.en_US
dc.identifier.citedreferenceMo. H., Winter, H. C., Van Damme, E. J. M., Peumans, W. J., Misaki, A. & Goldstein, I. J. ( 2001 ) Carbohydrate binding properties of banana ( Musa acuminata ) lectin I. Novel recognition of internal α1–3 linked glucosyl residues. Eur. J. Biochem. 268, 2609 – 2615.en_US
dc.identifier.citedreferenceCunningham, B. A., Wang, J. L., Waxdal, M. J. & Edelman, G. M. ( 1975 ) The covalent and three-dimensional structure of concanavalin A. II. Amino acid sequence of cyanogen bromide fragment F3. J. Biol. Chem. 250, 1503 – 1512.en_US
dc.identifier.citedreferenceNomura, K., Ashida, H., Uemura, N., Kushibe, S., Ozaki, T. & Yoshida, M. ( 1998 ) Purification and characterization of a mannose/glucose-specific lectin from Castanea crenata. Phytochemistry 49, 667 – 673.en_US
dc.identifier.citedreferenceNomura, K., Nakamura, S., Fujitake, M. & Nakanishi, T. ( 2000 ) Complete amino acid sequence of Japanese chestnuts agglutinin. Biochem. Biophys. Res. Comm. 276, 23 – 28.en_US
dc.identifier.citedreferenceVan Damme, E. J. M., Barre, A., Verhaert, P., Rouge, P. & Peumans, W. J. ( 1996 ) Molecular cloning of the mitogenic mannose/maltose-specific rhizome lectin from Calystegia sepium. FEBS Lett. 397, 352 – 356.en_US
dc.identifier.citedreferenceVan Damme, E. M. J., Barre, A., Mazard, A. M., Verhaert, P., Horman, A., Debray, H., Rouge, P. & Peumans, W. J. ( 1999 ) Characterization and molecular cloning of the lectin from Helianthus tuberosus. Eur. J. Biochem. 259, 135 – 142.en_US
dc.identifier.citedreferenceBourne, Y., Zaboni, V., Barre, A., Peumans, W. J., Van Damme, E. M. J. & Rouge, P. ( 1999 ) Helianthus tuberosus lectin reveals a widespread scaffold for mannose-binding lectins. Structure 7, 1473 – 1482.en_US
dc.identifier.citedreferencePeumans, W. J., Winter, H. C., Bemer, V., Van Leuven, F., Goldstein, I. J., Truffa-Bachi, P. & Van Damme, E. J. M. ( 1997 ) Isolation of a novel plant lectin with an unusual specificity from Calystegia sepium. Glycoconjugate J. 14, 259 – 265.en_US
dc.identifier.citedreferenceGoldstein, I. J., Winter, H. C., Mo. H., Misaki, A., Van Damme, E. J. M. & Peumans, W. J. ( 2001 ) Carbohydrate binding properties of banana ( Musa acuminata ) lectin II. Binding of laminaribiose oligosaccharides and β-glucans containing β-1,6-glucosyl end groups. Eur. J. Biochem. 268, 2616 – 2619.en_US
dc.identifier.citedreferenceHase, S., Sugimoto, T., Takemoto, H., Ikenaka, T. & Schmid, K. ( 1986 ) The structure of sugar chains of Japanese quail ovomucoid. The occurrence of oligosaccharides not expected from the classical biosynthetic pathway for N-glycans; A method for the assessment of the structure of glycans present in picomolar amount. J. Biochem. 99, 1725 – 1733.en_US
dc.identifier.citedreferencePeumans, W. J., Zhang, W., Barre, A., Houles Astoul, C., Balint-Kurti, P. J., Robia, P., Rouge, P., May, G. D., Van Leuven, F., Truffa-Bachi, P. & Van Damme, E. J. M. ( 2000 ) Fruit-specific lectins from banana and plantain. Planta 211, 546 – 554.en_US
dc.identifier.citedreferenceMann, K., Farias, C. M., Del Sol, F. G., Santos, C. F., Grangeiro, T. B., Nagano, C. S., Cavada, B. S. & Calvete, J. J. ( 2001 ) The amino acid sequence of the glucose/mannose-specific lectin isolated from Parkia platycephala seeds reveals three tandemly arranged jacalin-related domains. Eur. J. Biochem. 268, 4414 – 4422.en_US
dc.identifier.citedreferenceClaes, B., Dekeyser, R., Villarroel, R., Van Den Bulcke, M., Bauw, G., Van Montagu, M. & Caplan, A. ( 1990 ) Characterization of a rice gene showing organ-specific expression in response to salt stress and drought. Plant Cell 2, 19 – 27.en_US
dc.identifier.citedreferenceHirano, K., Teraoka, T., Yamanaka, H., Harashima, A., Kunisaki, A., Takahashi, H. & Hosokawa, D. ( 2000 ) Novel mannose-binding rice lectin composed of some isolectins and its relation to a stress-inducible salT gene. Plant Cell Physiol. 41, 258 – 267.en_US
dc.identifier.citedreferenceZhang, W., Peumans, W. J., Barre, A., Astoul, C. H., Robia, P., Rouge, P., Proost, P., May, G. D., Truffa-Bachi, P., Jalali, A. A. & Van Damme, E. J. M. ( 2000 ) Isolation and characterization of a jacalin-related mannose-binding lectin from salt-stressed rice ( Oryza sativa ). Planta 211, 970 – 978.en_US
dc.identifier.citedreferenceNagasawa, R., Yasokawa, D., Okumura, Y. & Nakajima, K. ( 2000 ) Cloning and sequence analysis of cDNA coding for a lectin from Helianthus tuberosus callus and its jasmonate-induced expression. Biosci. Biotechnol. Biochem. 64, 1247 – 1254.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


Files in this item

Name:
j.1432-1033.2002.03127.x.pdf
Size:
419.0KB
Format:
PDF
View/Open

Show simple item record

Remediation of Harmful Language

The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.

Accessibility

If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.