. The Biological bulletin. Biology; Zoology; Marine biology. 400 P. SCAPS ET AL. 12 3 4 5. both cases, much of the activity remained at the top of the gel. The apparent molecular weights of A^. diversicolor ChEs were 18,500 ± 3500; 47,000 ± 4500 and 55,000 ± 4400 (« = 3). A similar intensity was revealed with ATCh or PrTCh as substrate; no activity was found with BuTCh (Fig. 5 A). In E. fetida, the apparent molecular weights of the five bands moving into the gel were estimated to be 628,000 ± 19,730 (1); 310,000 ± 5470 (2); 235,000 ± 3200 (3); 106,000 ± 5300 (4); and 53,800 ± 7010 (5) (« = 5).
. The Biological bulletin. Biology; Zoology; Marine biology. 400 P. SCAPS ET AL. 12 3 4 5. both cases, much of the activity remained at the top of the gel. The apparent molecular weights of A^. diversicolor ChEs were 18,500 ± 3500; 47,000 ± 4500 and 55,000 ± 4400 (« = 3). A similar intensity was revealed with ATCh or PrTCh as substrate; no activity was found with BuTCh (Fig. 5 A). In E. fetida, the apparent molecular weights of the five bands moving into the gel were estimated to be 628,000 ± 19,730 (1); 310,000 ± 5470 (2); 235,000 ± 3200 (3); 106,000 ± 5300 (4); and 53,800 ± 7010 (5) (« = 5). The slowest moving band (band 1) had a variable density and was even absent from one experiment to an- other (Fig. 5B, lanes la, b), whereas the other bands de- veloped at a higher intensity with PrTCh than with ATCh or BuTCh as substrate (Fig. 5B, lanes lb, 2, 3). Bands 2, 3, and 5 were more intense with ATCh than with BuTCh as substrate, whereas band 4 had a higher density with BuTCh than with ATCh. 1a 1b 2 3 4 5 B Figure 4. Disc electrophoresis of ChEs from Nereis diversicolor (A) and Eisenia fetida (B) in polyacrylamide gels. Variation in staining reaction: (1) S fraction ATCh hydrolysis; (2) S fraction PrTCh hydrolysis; (3) S fraction BuTCh hydrolysis; (4) DS fraction ATCh hydrolysis; (5) S fraction eserine (10"' M) inhibition; (la and lb) variability in the in- tensity of band 1 with S fractions and ATCh hydrolysis. but not with the same intensity (weaker in the posterior part). Two isoenzymes were found in E. fetida. The first had a very variable density and was even absent in re- peated experiments (Fig. 4B, lanes la, b). The fastest moving band was more intense with PrTCh than with ATCh or BuTCh, which confirms the results with the Ell- man procedure. As in TV. diversicolor, a large amount of activity remained at the top of the gel (Fig. 4B). PAGGE gave, respectively, three and five bands of ac- tivity in N. diversicolor and in E. fetida (Fig. 5A,
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