. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. MARSH PHRIWINKLE ADHESIVE MUCUS 343. Figure 3. The effect of reducing agents on the proteins found in adhesive mucus. The sample in lane a was reduced prior to running on the gel. while the sample in lane c was not reduced. Molecular weight markers are in lane b and have the following weights: 205. 116, 97, 84, 66, 55, 45, and 36 kD. protein in the adhesive, yet they were not present in the trail mucus. The proteins found in the trail mucus were different from those found in the adhesive mucus. The main proteins were 65, 63.
. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. MARSH PHRIWINKLE ADHESIVE MUCUS 343. Figure 3. The effect of reducing agents on the proteins found in adhesive mucus. The sample in lane a was reduced prior to running on the gel. while the sample in lane c was not reduced. Molecular weight markers are in lane b and have the following weights: 205. 116, 97, 84, 66, 55, 45, and 36 kD. protein in the adhesive, yet they were not present in the trail mucus. The proteins found in the trail mucus were different from those found in the adhesive mucus. The main proteins were 65, 63. and 59 kD (Fig. 2). Bands in this range occasionally showed up in the adhesive mucus, but only in relatively small amounts. In both forms of mucus, there was no material at the top of or within the stacking gel, and there were only a few faint bands near the top of the resolving gel. Finally, the overall difference in protein concentration that was detected by the BCA assay was also apparent in the stained gels. Disulfide bonds affect the structure of the 41 and 36 kD proteins. When these bonds are not broken, the two primary bands show up at 64 and 59 kD (Fig. 3). Thus, disultkle bonds may change the protein structure or SDS binding to create a greater apparent molecular weight. Alternatively, the 41 and 36 kD proteins may be subunits of slightly larger proteins that are held together by disulfide bonds. The key finding, though, is that the proteins are not linked into giant complexes, unlike mammalian mucin. With disulfide bonds intact, there were faint bands at a lower molecular weight, but no significant bands above 64 kD in the resolving or stacking gel. PAS staining showed that most of the carbohydrates in the mucus appear to be in the form of very large molecules (Fig. 4). There was distinct staining in the stacking gel or at the interface between the stacking and resolving gels. There was faint staining at the position of the 41 kD protein, but it was barely visible. V
Size: 1488px × 1678px
Photo credit: © Library Book Collection / Alamy / Afripics
License: Licensed
Model Released: No
Keywords: ., bookauthorlilliefrankrat, booksubjectbiology, booksubjectzoology
