A comparative study of the change in diatom inferred ph of a staircase of lakes in the Algoma District, Northern Ontario /

Four staircase lakes occupying a single watershed located in the Algoma District, north of Lake Superior were chosen for this study. I examined the subfossil diatom assemblage in the top twenty centimeters of the surface sediments in each of these four lakes in an attempt to reconstruct their respective past pH history. From these analyses it was possible to test the hypothesis that the rate of change of diatom inferred pH was not significantly different in lakes located one below the other in a single "staircase" within a single watershed system. My results indicated that the four Z lakes had been acid for at least the last century. The water color of the three upper Z lakes (Z1, Z2 and Z3) was brown (>30 Pt Co units). The bottom lake (Z4) was the only clear water lake in the system «5 Pt Co units). This bottom staircase lake had no muskeg development around its shoreline. The alkaliphilous diatoms in the Z watershed system were important in determining the diatom inferred pH of the four Z lakes. The centric diatoms were extremely rare in the clearwater bottom lake (Z4). The ecology of the Eupodiscales is perhaps important in the interpretation of sediment in the more acid environment. Lake Z4 was the only one that had a progressive as well as a significant decrease in its downcore diatom inferred pH since the early 1960's. This lead me to speculate that the humic substances present in the upper three brown water lakes (Z1, Z2 and Z3) were perhaps Important in buffering them against a further decrease in water pH even though they were located within an area which was sensitive to acid precipitation.

Isolation and partial characterization of host cell wall surface glycoproteins: their involvement in agglutination, attachment and appressorium formation by piptocephalis virginiana

Cell surface proteins obtained by alkaline extraction from isolated cell walls of Mortierella pusilla and M. candelabrum, host and nonhost, respectively, to the mycoparasite, Piptocephalis virginiana, were tested for their ability to agglutinate mycoparasite spores. The host cell wall protein extract had a high agglutinating activity (788 a.u. mg- t ) as compared with the nonhost extract (21 a.li. mg- t ). SDS-polyacrylamide gel electrophoresis of the cell wall proteins revealed four protein bands, a, b, c, and d (Mr 117, 100, 85 and 64 kd, respectively) at the host surface, but not at the nonhost surface, except for the faint band c. Deletion of proteins b or c from the host cell wall protein extract significantly reduced its agglutinating activity. Proteins band c, obtained as purified preparations by a series of procedures, were shown to be two glycoproteins. Carbohydrate analysis by gas chromatography demonstrated that glucose and Nacetylglucosamine were the major carbohydrate components of the glycoproteins. It was further shown that the agglutinating activity of the pure preparation containing both band c was 500-850 times that of the single glycoproteins, suggesting the involvement of both glycoproteins in agglutination. The results suggest that the glycoproteins band c are the two subunits of agglutinin present at the host cell surface. The two glycoproteins band c purified from the host cell wall protein extract were further examined after various treatments for their possible role in agglutination, attachment and appressorium formation by the mycoparasite. Results obtained by agglutination and attachment tests showed: (1) the two glycoprotein-s are not only an agglutinin responsible for the mycoparasite spore agglutination, but may also serve as a receptor for the specific recognition, attachment and appressorium formation by the mycoparasite; (2) treatment of the rnycoparasite spores with various sugars revealed that arabinose, glucose and N-acetylglucosamine inhibited the agglutination and attachment activity of the glycoproteins, however, the relative percentage of appressorium formation was not affected by the above sugars; (3) the two glycoproteins are relatively stable with respect to their agglutinin and receptor functions. The present results suggest that the agglutination and attachment may be mediated directly by certain sugars present at the host and mycoparasite cell surfaces while the appressorlum formation may be the response of complementary combinations of both sugar and protein, the two parts of the glycoproteins at the interacting surfaces of two fungi.