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Immobilized Cratylia mollis lectin: An affinity matrix to purify a soybean (Glycine max) seed protein with in vitro platelet antiaggregation and anticoagulant activities

Paper ID Volume ID Publish Year Pages File Format Full-Text
35357 45088 2011 7 PDF Available
Title
Immobilized Cratylia mollis lectin: An affinity matrix to purify a soybean (Glycine max) seed protein with in vitro platelet antiaggregation and anticoagulant activities
Abstract

Lectins, proteins which recognize selectively carbohydrates, have been used as affinity chromatography to purify glycoproteins. Cratylia mollis seed lectin (Cramoll 1,4), of mannose/glucose binding class, immobilized on Sepharose CL-4B, was used as affinity matrix. This paper describes the purification by Cramoll 1,4-Sepharose matrix, and characterization of an anti-platelet and anticoagulant soybean (Glycine max) protein, ApcSP, and its in vitro platelet antiaggregation and anticoagulant activities. SDS-PAGE of ApcSP purified under reducing condition revealed a single glycosilated band of 51 kDa. The N-terminal 10-residue sequence of ApcSP is EGQFGPMIQS, distinct to other soybean seed proteins, such as peroxidase, lectin, 2S albumin and trypsin inhibitor. Deconvolution of CD spectrum indicated 35% α-helix, 17% β-strand, 22% turn and 26% unordered structure; ApcSP fluorescence spectrum showed a maximum emission around 339 nm. The hemostatic parameters revealed inhibition of collagen (p < 0.001), thrombin (p < 0.05) and ADP (p < 0.001)-induced platelet aggregation in the presence of ApcSP (2 μM), in relation to positive control. The soy protein prolonged the blood coagulation time (activated partial thromboplastin time, more affected, and prothrombin time). The results indicated that immobilized Cramoll 1,4 lectin has the potential to isolate soybean glycoproteins and ApcSP may be important for anti-thrombotic and anticoagulant therapy.

Keywords
Antiaggregant; Anticoagulant; Cramoll 1,4-Sepharose; Glycine max; Glycoprotein; Lectin
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Immobilized Cratylia mollis lectin: An affinity matrix to purify a soybean (Glycine max) seed protein with in vitro platelet antiaggregation and anticoagulant activities
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 46, Issue 1, January 2011, Pages 74–80
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us