Exoprotease Production by Aeromonas hydrophila in a Chemically Defined Medium Page: 56
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56
was calculated as the ratio of distance of migration of
test material to that of the dye front (R ). The mobili-
ties of each standard protein were plotted against the log0
of its molecular weight. The unknown molecular weight of
the protease was determined by finding its R on the stand-
ard curve and reading the log10 of its molecular weight
from the ordinate. The antilog of this number is the mo-
lecular weight of the protease. Protease I had five faint-
ly staining bands and one heavy staining band in the gel.
The molecular weights of the faint bands were 43,700; 26,900;
25,700; 21,400; and 14,800. The heavy band had a molecular
weight of 18,600 (Figure 9). The molecular weight of pro-
tease II was 19,500 (Figure 10).
Hemolytic Assay
The hemolytic activity of protease II was higher than pro-
tease I when both were incubated for 1 hour (Figure 11 and
12). Protease II had a maximum hemolytic activity at the
1:128 dilution when the assay was incubated for 1 hour.
There is only a small amount of hemolytic activity noted in
protease I (Figure 11).
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Anderson, Paulette S. (Paulette Sue), 1952-. Exoprotease Production by Aeromonas hydrophila in a Chemically Defined Medium, thesis, May 1985; Denton, Texas. (https://digital.library.unt.edu/ark:/67531/metadc504602/m1/61/: accessed April 23, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; .