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  <record>
    <language>eng</language>
          <publisher>Oriental Scientific Publishing Company</publisher>
        <journalTitle>Biosciences Biotechnology Research Asia</journalTitle>
          <issn>0973-1245</issn>
            <publicationDate>2026-03-30</publicationDate>
    
        <volume>23</volume>
        <issue>1</issue>

 
    <startPage>41</startPage>
    <endPage>50</endPage>

	 
      <doi>10.13005/bbra/3479</doi>
        <publisherRecordId>58348</publisherRecordId>
    <documentType>article</documentType>
    <title language="eng">Characterization of a Mannose-Binding Seed Lectin from Trigonella foenum-graecum with Broad Erythrocyte Agglutination</title>

    <authors>
	 


      <author>
       <name>Suresh Basavaraj Arakera</name>

 
		
	<affiliationId>1</affiliationId>
      </author>
    

	 


      <author>
       <name>Vinuta Hanamant Mane</name>


		
	<affiliationId>1</affiliationId>

      </author>
    

	 


      <author>
       <name>Shubhangi Pingle</name>

		
	<affiliationId>2</affiliationId>
      </author>
    

	


	


	
    </authors>
    
	    <affiliationsList>
	    
		
		<affiliationName affiliationId="1">Molecular Medicine and Microbial Genetics Laboratory, Department of Applied Genetics, Karnatak University, Pavatenagar, Karnataka, India.</affiliationName>
    

		
		<affiliationName affiliationId="2">Regional Occupational Health Centre, ICMR Institute Devanahalli Bengaluru, Karnataka, India. </affiliationName>
    
		
		
		
		
	  </affiliationsList>






    <abstract language="eng">Lectins are carbohydrate-binding proteins widely distributed in leguminous plants and are known for their hemagglutination and diverse biological activities; in this study, a mannose-specific lectin was isolated and partially characterized from Trigonella foenum-graecum seeds by extraction with phosphate-buffered saline, partial purification through ammonium sulphate precipitation and dialysis, and characterization using hemagglutination, sugar inhibition assays, pH and temperature stability tests, and SDS-PAGE analysis. The lectin exhibited strong hemagglutination activity against human A, B, and O erythrocytes without strict blood-group specificity, and its activity was selectively inhibited by mannose, confirming its mannose specificity. The lectin remained stable within a pH range of 6–8 and at temperatures up to 70°C, while SDS-PAGE revealed a protein band of approximately 28–30 kDa. Overall, the findings indicate that Trigonella foenum-graecum seeds are a rich source of a stable mannose-specific lectin with significant potential applications in glycobiology and biomedical research.</abstract>

    <fullTextUrl format="html">https://www.biotech-asia.org/vol23no1/characterization-of-a-mannose-binding-seed-lectin-from-trigonella-foenum-graecum-with-broad-erythrocyte-agglutination/</fullTextUrl>



      <keywords language="eng">
        <keyword>Hemagglutination; pH; Sugar specificity; Temperature stability; Trigonella foenum-graecum</keyword>
      </keywords>

  </record>
</records>