Figure 1.
Affinity purification of A. gorakhpurensis lectin on mucin-Sepharose 4B column.
Fractions (1.0 mL) were collected and analyzed for protein content and titre.
Figure 2.
Sodium Dodecyl Sulphate-Polyacrylamide Gel of A. gorakhpurensis lectin.
Lane 1: Molecular weight markers from top: myosin (201.2 kDa); β-galactosidase (120.3 kDa); bovine serum albumin (100.2 kDa); ovalbumin (55.9 kDa); carbonic anhydrase (38.3 kDa); soyabean trypsin inhibitor (29.7 kDa) and lysozyme (20.7 kDa), Lane 2: Porcine stomach mucin-Sepharose 4B fraction, Lane 3: Crude.
Figure 3.
a. Molecular mass determination of purified A. gorakhpurensis lectin by gel filtration chromatography on Sephadex G-100 column.
(a) Conalbumin 75 kDa, (b) Ovalbumin 44 kDa, (c) Carbonic anhydrase 29 kDa, (d) Ribonuclease A 13.7 kDa, (e) Aprotinin 6.5 kDa. b. Elution profile of A. gorakhpurensis lectin on Sephadex G-100 column.
Figure 4.
Molecular mass determination of A. gorakhpurensis lectin by MALDI-TOF.
Table 1.
Summary of purification of A. gorakhpurensis lectin.
Figure 5.
Mitogenic response of mouse splenocytes to purified A. gorakhpurensis lectin.
Con A, Concanavalin A lectin (Positive control); Neg, Negative control (Cells without the addition of any mitogen). Data is presented as Mean ± SD.
Table 2.
Antimicrobial activity of purified A. gorakhpurensis lectin.