. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. 2B Figure 2. Proteins extracted from the cephulothoracic shield cuticle of anecdysial Carcinus niacnus. Silver-stained SDS-polyacrylamide gels (15%). 50 /xg protein/lane. Fig. 2A. Lane 1: 2% HAc-extract; Lane 2: N HCI-extract; Lane 3: 10% EDTA-extract: Lane 4: M KCl-extract: Lanes M; Molecular Weight Marker 10 kDa Protein Ladder (GibcoBRL). Fig. 2B. Densitometric profiles of the HCI- and EDTA-extracts lanes (2 and 3). resembled that of the HCI extract in the low-MW ranges, but in the high- and medium-MW ranges, many
. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. 2B Figure 2. Proteins extracted from the cephulothoracic shield cuticle of anecdysial Carcinus niacnus. Silver-stained SDS-polyacrylamide gels (15%). 50 /xg protein/lane. Fig. 2A. Lane 1: 2% HAc-extract; Lane 2: N HCI-extract; Lane 3: 10% EDTA-extract: Lane 4: M KCl-extract: Lanes M; Molecular Weight Marker 10 kDa Protein Ladder (GibcoBRL). Fig. 2B. Densitometric profiles of the HCI- and EDTA-extracts lanes (2 and 3). resembled that of the HCI extract in the low-MW ranges, but in the high- and medium-MW ranges, many bands were missing or very faint. As mentioned above, the staining intensity of a protein band could vary drastically with the gel staining method. The 17-kDa band of the HAc and HCI extracts, for instance, was stained only by silver (Fig. 2), and the 16-kDa band that was intensely stained by Coomassie blue whatever the ex- tract (Fig. 1) was not revealed by silver staining (Fig. 2). Reaction of extracted proteins with lectins Lectin binding revealed that most of the proteins ex- tracted by the described procedure are glycosylated. The labeling intensity varied, however, according to the protein band and the lectin used. Conspicuous differences were again observed between neutral- and acidic-solvent extracts. Concanavalin A. Of the five lectins tested. Con A labeled the greatest number of protein bands (Fig. 3). Almost all the protein bands in the high- and medium-MW ranges bound Con A, suggesting that they are glycosylated, primarily with mannose. In these ranges, only a few differences were observed between the various extracts ( differences in the intensity of some high-MW bands between acidic- and neutral-solvent extracts). The bands exhibiting the strongest Con A binding were mostly those staining intensely with Coomassie blue or silver. The 200-kDa band appeared to be labeled in every extract lane, even when it did not appear, or was very faint, after Coomassie or si
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