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Physical studies on three lectins from the seeds of Abrus precatorius
Affiliation:1. Qingdao Agricultural University, Qingdao 266109, PR China;2. Department of Physics, Pukyong National University, Busan 608-737, Republic of Korea;1. Institute of Physical Chemistry, Polish Academy of Sciences, ul. Kasprzaka 44/52, 01-224 Warszawa, Poland;2. Organic Materials and Interfaces, Department of Chemical Engineering, Delft University of Technology, Delft, Netherlands;3. Faculty of Chemistry, University of Warsaw, Pasteura 1 Str. 02-093 Warsaw, Poland;1. Department of Physics, Indian Institute of Technology Guwahati, Guwahati, Assam, 781039, India;2. Department of Physics, Manipal University, Jaipur, RJ, 303007, India;3. Indo-Korea Science and Technology Center (IKST), New Airport Road, Yelahanka, 560065, Bangalore, India;1. Department of Radiology, the Second Hospital of Jilin University, Changchun 130041, China;2. State Key Laboratory of Inorganic Synthesis and Preparation & Preparative Chemistry, Jilin University, Changchun 130012, China;3. Department of Pathology, the Second Hospital of Jilin University, Changchun 130041, China;4. Department of Radiology, the Second Hospital of Chongqing Medical University, Chongqing 400010, China;1. Laboratório Integrado de Biomoléculas – LIBS, Departamento de Patologia e Medicina Legal, Universidade Federal do Ceará, 60430-160, Fortaleza, Ceará, Brazil;2. Departamento de Ciências Biológicas, Faculdade de Ciências Exatas e Naturais, Universidade do Estado do Rio Grande do Norte, 59625-620, Mossoró, Rio Grande do Norte, Brazil;3. Laboratório de Biotecnologia Molecular (LabBMol), Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, 60455-970, Fortaleza, Ceará, Brazil;4. Curso de Ciências Biológicas, Universidade Estadual Vale do Acaraú, 62040-370, Sobral, Ceará, Brazil;5. Departamento de Engenharia de Pesca, Universidade Federal do Ceará, 60356-000, Fortaleza, Ceará, Brazil
Abstract:The physical properties of three lectins from the seeds of the Abrus precatorius plant, abrin C, abrin A and the Abrus agglutinin, were studied. All three exhibited similar circular dichroic (CD) spectra in the near-ultraviolet having negative maxima at 286 and 293 nm. In addition, d-galactose induced similar conformational alterations in the three proteins as observed through changes in the near-ultraviolet CD from 280 to 295 nm. The near-ultraviolet CD spectrum of the toxic subunit of abrin C was very different from that of the parent molecule. The fluorescence emission spectra of the three proteins were also studied. All exhibited fluorescence near 335 nm which is quenched 9% by galactose. Iodide quenching of fluorescence using the Stern-Volmer analysis indicated different tryptophan accessibilities in the presence and absence of d-galactose for the Abrus agglutinin. The result suggest that there is a saccharide-induced conformational change which buries several partially exposed tryptophan residues. A comparable analysis of the closely related Ricinus agglutinin revealed that its tryptophan residues are more buried than those of the Abrus agglutinin and, unlike the Abrus agglutinin, there was no saccharide-induced change in tryptophan accessibility.
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