PROGRESS IN PROTOZOOLOGY

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260 D. L. NANNEY Esterase-1 is a propionyl esterase, activated by sodium taurocholate and inhibited by eserine sulfate. Esterase-2 is a butyryl esterase activated by p-chloromercuribenzoate and insensitive to eserine. Finally esterase-3 acts on both a-naphthyl propionate and butyrate; it is activated by both sodium taurocholate and p-chloromercuribenzoate and is insensitive to eserine. These specifications seemed suitable for identifying the arrays of isozymes in the various species. However, the esterases differ not only in their electrophoretic mobilities but also in their other enzymatic characteristics. Three species manifested isozymes of all three classes, but in the other species one or more of the classes is missing entirely. T. pigmentosa and T. hyperangularis have no enzymes that can be unequivocally associated with esterases-1, -2, or -3. These observations do not prove that homologous proteins are missing from the other species, or even that the homologous proteins are no longer esterases. They do demonstrate that some of the functional characteristics of these enzymes are labile within the complex, despite the superficial physiological and nutritional similarities of the organisms. Simply to show that the variability of the esterases is no isolated example, consider for a moment the results of a recently published (Nanney et al. 1981) starch gel electrophoretic analysis of the NADPisocitrate dehydrogenase enzymes. T. pigmentosa (Table 11) manifests three isozymes — a proximal, a middle and a distal band. Other species show one, two, or three bands, and their positions within the general region in which they appear are variable. We can arbitrarily classify a species as to the isozymes present (or absent) within each region of the gel, and as to their relative mobility (fast or slow). Although this procedure provides "characters" that can be used in sorting the species, we cannot be confident of the genetic relationships of the molecules being compared. This enzyme may be somewhat more evolutionarily constrained than are the esterases, but not much more. The enzyme's lability is too great for it to be used as a reliable measure of evolutionary distance in species so distantly removed from a common ancestor. This same conclusion is probably appropriate for isozymic studies on several other enzymes (Borden et al. 1977); in many cases one simply cannot compare the electrophoretic mobility of enzymes for two species, because the enzymes are too different to be visualized under the same circumstances on a gel. Such data may be helpful for taxonomic purposes, in the identification of a species; they are probably useless in defining phylogenetic relationships. Primarily because the form of Tetrahymena is so perfectly preserved in all the species of the complex, one might suppose that structural proteins would be more conservative in this group than are many of the http://rcin.org.pl
THE MOLECULAR DIVERSITY OF TETRAHYMENA PYRIFORMIS 261 Table 11 Relative electrophoretic mobilities of isocitrate dehydrogenase (IDH) isozymes in Tetrahymena species. Symbols in parentheses indicate weak and irregularly observed bands. F refers to fast migrating bands, S to slowly migrating bands Species Proximal Band Middle Band Distal Band Sum- 5-10 11-17 45-55 56-68 99-110 111-123 mary Amicronucleate species T. pyriformis (A) T. elliotti (B) _L + + + OFF OSS T. jurgasoni (C) OSO T. Iwoffi (E) Micronucleate species (+) OSO T. thermophila (1) T. americanis (2) + + + + OSS SOS T. borealis (3) T. hegewischi (5) T. canadensis (7) (6) T. pigmentosa W T. tropicalis (9) T. hyperangutaris (10) T. austra/is (11) T. capricornis (12) T. sonneborni (13) T. nipissingi (14) + (+) T (+) (+) (+) + + J. + + (+) (+) (+) + (+) + + + + + + + + -j- + + SOS FFS SFF SFF FFF SFS SOS SOS OOF FSS FFS N a n n e y et al. (1981). catalytic proteins. Indeed some structural proteins are very conservative, at least in some respects. Vaudaux et al. (1977) extracted the major cortical proteins of a number of species of Tetrahymena and separated them according to molecular weight (Table 12). All the species, including two of the T. patula complex, had a protein of high molecular weight of about 250 000 daltons. All species also had one or two smaller proteins, falling into a limited number of molecular weight classes. The patterns yield to no simple evolutionary scheme, primarily because of the similar patterns expressed within and outside the species complex. Obviously the system of proteins is highly constrained with respect to molecular weight classes, but the architectural rationale or the evolutionary basis of the constraint is obscure. Species with the same patterns are not necessarily more closely related. Another study of structural proteins also gives evidence of some unexpected molecular conservatism in the face of large scale variability. Seyfert and Willis (1981) extracted the proteins of the cilia of five species of the T. pyriformis complex and studied their molecular weights by SDS-polyacrylamide gel electrophoresis. Over 30 polypeptides http://rcin.org.pl
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POLISH ACADEMY OF SCIENCES NENCKI I
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PROGRESS IN PROTOZOOLOGY Proceeding
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INTRODUCTORY REMARKS This Part II o
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183 In his abstract Mignot (1981) s
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187 algae by phycologists (Bourelly
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195 The foregoing subdivisions of A
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Page 41 and 42: REFERENCES 215 Bardele C. F. 1977:
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Page 51 and 52: 225 brate cycle in vitro. Further c
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Page 55 and 56: 229 for the development of methods
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Page 59 and 60: Malaria IN VITRO CULTIVATION OF PAR
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Page 63 and 64: 237 Rai Choudhuri A. N.. Chowdhuri
Page 67 and 68: 241 Only those with 9-type 1 fronto
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Page 73 and 74: 247 in eukaryotes. It is about the
Page 75 and 76: Table 2 Mating species of Tetrahyme
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Page 91 and 92: 265 Cuny M., Milet M. and Hayes D.
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Page 123 and 124: 293 Co-Chairman: Jan Kućera, Czech
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LONDON 1965 http://rcin.org.pl
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CONTENTS Introductory Remarks 179 B
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