268. Tiedtke A.: Purification and properties of secreted Nactyl-B-D-hexosaminidase of Tetrahymena thermophila. Compo Biochem. Physiol. Pt. B 75: 239-243
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269. Trainer D. G. and Tillinghast E. K.: Amylolytic activity of the crystalline style of Mya arenaria (Bivalvia,
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99-103 (1982)
270. Trezise A. E. O. et al.: Cloning and sequencing of
cDNA encoding baboon liver alcohol dehydrogenase:
Evidence for a common ancestral lineage with the
human alcohol dehydrogenase ~ subunit and for class
I ADH gene duplications. Proc. Nat. Acad. Sci. USA
86: 5454-58 (1989)
271. Tsai C. S. et ai.: Purification and comparative studies
of alcohol dehydrogenases. Compo Biochem. Physiol.
Pt. B 87: 79-85 (1987)
272. Tsukada T. and Yoshino M.: ~-Glucuronidase from
Ampullaria. Purification and kinetic properties.
Compo Biochem. Physiol. Pt. B 86: 565-569 (1987)
273. Turnbull J. E. and Gallagher J. T.: Sequence analysis
of heparan sulphate indicates defined location of Nsulphated glucosamine and iduronate 2-sulphate residues proximal to the protein-linkage region. Biochern. J. 277: 297-303 (1991)
274. Ueno R. and Yuan C. S.: Purification and properties
of neutral ~-N-acetylglucosaminidase from carp
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275. Usanga E. A. and LuzzaUo L.: Adaptation of Plasmodium
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(1985)
276. Vaandrager S. H. et al.: Fractionation and kinetic
properties of trehalase from flight muscles and haemolymph of the locust, Locusta migratoria. Insect
Biochem. 19: 89-94 (1989)
277. Vanderzel A. et al.: The involvement of catalase in
alcohol metabolism in Drosophila melanogaster larvae. Arch. Biochem. Biophys. 287: 121-127 (1991)
278. Veivers P. c., O'Brien R. Wand Siaytor M.: Selective defaunation of Mastotermes darwiniensis and its
effect on cellulose and starch digestion. Insect Biochern. 13: 95-101 (1983)
279. Vieira R. P., Mulloy B. and Mourao P. A. S.: Structure of a fucose-branched chondroitin sulfate from
sea cucumber. Evidence for the presence of 3-0sulfo-B-D-glucuronyl residues. J. BioI. Chern. 266:
13530-36 (1991)
280. Villarroya A.: The primary structure of alcohol
dehydrogenase from Drosophila lebanonensis.
Extensive variation within insect "short chain" alcohol dehydrogenase lacking zinc. Eur. J. Biochem.
180: 191-197 (1989)
281. Vilotte J. L. et al.: Sequence of the goat a-lactalbumin-encoding gene: Comparison with the bovine
gene and evidence of related sequences in the goat
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282. VUlliamy T. J. et ai.: Diverse point mutations in the
human glucose-6-phosphate dehydrogenase gene
cause enzyme deficiency and mild or severe hemolytic
References
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anemia. Proc. Nat. Acad. Sci. USA 85: 5171-75
(1988)
283. Vynios D. H. and Tsiganos C. P.: Squid proteoglycans: Isolation and characterization of three populations from cranial cartilage. Biochim. biophys. Acta
1033: 139-147 (1990)
284. Wakita M. and Hoshino S.: Physicochemical properties of a reserve polysaccharide from sheep rumen
ciliates genus Entodinium. Compo Biochem. Physiol.
Pt. B 65: 571-574 (1980)
285. Wallace C. A. et al.: L-Gulonolactone oxidase is present in the invertebrate, Limulus polyphemus.
Experientia 41: 485-486 (1985)
286. Weaver J. R., Andrews J. M. and Sullivan D. T.: Nucleotide sequence of the Adh-l gene of Drosophila
navojoa. Nucleic Acids Res. 17: 7524 (1989)
287. Weisman L. S., Krummel B. M. and Wilson A. c.:
Evolutionary shift in the site of cleavage of prelysozyme. J. bioI. Chern. 261: 2309-13 (1986)
288. White J. W: Honey. Adv. Food Res. 24: 287-374
(1978)
289. Wiebauer K. et al.: A 78-kilobase region of mouse
chromosome 3 contains salivary and pancreatic amylase genes and a pseudogene. Proc. Nat. Acad. Sci.
USA 82: 5446-49 (1985)
290. Winberg J. O. et al.: Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis.
Biochem. J. 235: 481-490 (1986)
291. Wolfenson C. and de Lederkremer R. M.: Purification and composition of glycoconjugates from Crithidia oncopelti. Comp. Biochem. Physiol. Pt. B 77:
555-560 (1984)
292. Xavier M. T. et ai.: Chemical structures of a galactose-rich glycoprotein of Leishmania tarentolae. Compo
Biochem. Physiol. Pt. B 88: 101-104 (1987)
293. Yamasaki K.: Characterization and partial purification of a mannanlike polysaccharide in the eggs of
Locusta migratoria. Insect Biochem. 3: 79-90
(1973)
294. Yet M. G. and Wold E: The distribution of glycan
structures in individual N-glycosylation sites in animal
and plant glycoproteins. Arch. Biochem. Biophys.
278: 356-364 (1990)
295. Yokota K., Nishi Y. and Takesue Y.: Purification and
characterization of amphiphilic trehalase from rabbit
small intestine. Biochim. biophys. Acta 881: 405-414
(1986)
296. Zachary D. and Hoffmann D.: Lysozyme is stored in
the granules of certain haemocyte types in Locusta. J.
Insect Physiol. 30: 405-411 (1984)
297. Zera A. J., Koehn R. K. and Hall J. G.: Allozymes
and biological adaptation. In: Kerkut G. A. and Gilbert L. I. (eds.): Comprehensive insect physiology,
biochemistry and pharmacology, Vol. 10, pp.
633-674. Pergamon Press, Oxford 1985
298. Zhang W et al.: Primary structure of rabbit skeletal
muscle glycogen synthase deduced from cDNA clones. Faseb J. 3: 2532-36 (1989)
299. Zinkler D., Gotze M. and Fabian K.: Cellulose digestion in "primitive insects" (Apterygota) and oribatid
mites. Zool. Beitr. N. E 30: 17-28 (1986)
(1983)
269. Trainer D. G. and Tillinghast E. K.: Amylolytic activity of the crystalline style of Mya arenaria (Bivalvia,
Mollusca). Compo Biochem. Physiol. Pt. A 72:
99-103 (1982)
270. Trezise A. E. O. et al.: Cloning and sequencing of
cDNA encoding baboon liver alcohol dehydrogenase:
Evidence for a common ancestral lineage with the
human alcohol dehydrogenase ~ subunit and for class
I ADH gene duplications. Proc. Nat. Acad. Sci. USA
86: 5454-58 (1989)
271. Tsai C. S. et ai.: Purification and comparative studies
of alcohol dehydrogenases. Compo Biochem. Physiol.
Pt. B 87: 79-85 (1987)
272. Tsukada T. and Yoshino M.: ~-Glucuronidase from
Ampullaria. Purification and kinetic properties.
Compo Biochem. Physiol. Pt. B 86: 565-569 (1987)
273. Turnbull J. E. and Gallagher J. T.: Sequence analysis
of heparan sulphate indicates defined location of Nsulphated glucosamine and iduronate 2-sulphate residues proximal to the protein-linkage region. Biochern. J. 277: 297-303 (1991)
274. Ueno R. and Yuan C. S.: Purification and properties
of neutral ~-N-acetylglucosaminidase from carp
blood. Biochim. biophys. Acta 1074: 79-84 (1991)
275. Usanga E. A. and LuzzaUo L.: Adaptation of Plasmodium
falciparum
to
glucose-6-phosphate
dehydrogenase-deficient host red cells by production
of parasite-encoded enzyme. Nature 313: 793-795
(1985)
276. Vaandrager S. H. et al.: Fractionation and kinetic
properties of trehalase from flight muscles and haemolymph of the locust, Locusta migratoria. Insect
Biochem. 19: 89-94 (1989)
277. Vanderzel A. et al.: The involvement of catalase in
alcohol metabolism in Drosophila melanogaster larvae. Arch. Biochem. Biophys. 287: 121-127 (1991)
278. Veivers P. c., O'Brien R. Wand Siaytor M.: Selective defaunation of Mastotermes darwiniensis and its
effect on cellulose and starch digestion. Insect Biochern. 13: 95-101 (1983)
279. Vieira R. P., Mulloy B. and Mourao P. A. S.: Structure of a fucose-branched chondroitin sulfate from
sea cucumber. Evidence for the presence of 3-0sulfo-B-D-glucuronyl residues. J. BioI. Chern. 266:
13530-36 (1991)
280. Villarroya A.: The primary structure of alcohol
dehydrogenase from Drosophila lebanonensis.
Extensive variation within insect "short chain" alcohol dehydrogenase lacking zinc. Eur. J. Biochem.
180: 191-197 (1989)
281. Vilotte J. L. et al.: Sequence of the goat a-lactalbumin-encoding gene: Comparison with the bovine
gene and evidence of related sequences in the goat
genome. Gene 98: 271-276 (1991)
282. VUlliamy T. J. et ai.: Diverse point mutations in the
human glucose-6-phosphate dehydrogenase gene
cause enzyme deficiency and mild or severe hemolytic
References
513
anemia. Proc. Nat. Acad. Sci. USA 85: 5171-75
(1988)
283. Vynios D. H. and Tsiganos C. P.: Squid proteoglycans: Isolation and characterization of three populations from cranial cartilage. Biochim. biophys. Acta
1033: 139-147 (1990)
284. Wakita M. and Hoshino S.: Physicochemical properties of a reserve polysaccharide from sheep rumen
ciliates genus Entodinium. Compo Biochem. Physiol.
Pt. B 65: 571-574 (1980)
285. Wallace C. A. et al.: L-Gulonolactone oxidase is present in the invertebrate, Limulus polyphemus.
Experientia 41: 485-486 (1985)
286. Weaver J. R., Andrews J. M. and Sullivan D. T.: Nucleotide sequence of the Adh-l gene of Drosophila
navojoa. Nucleic Acids Res. 17: 7524 (1989)
287. Weisman L. S., Krummel B. M. and Wilson A. c.:
Evolutionary shift in the site of cleavage of prelysozyme. J. bioI. Chern. 261: 2309-13 (1986)
288. White J. W: Honey. Adv. Food Res. 24: 287-374
(1978)
289. Wiebauer K. et al.: A 78-kilobase region of mouse
chromosome 3 contains salivary and pancreatic amylase genes and a pseudogene. Proc. Nat. Acad. Sci.
USA 82: 5446-49 (1985)
290. Winberg J. O. et al.: Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis.
Biochem. J. 235: 481-490 (1986)
291. Wolfenson C. and de Lederkremer R. M.: Purification and composition of glycoconjugates from Crithidia oncopelti. Comp. Biochem. Physiol. Pt. B 77:
555-560 (1984)
292. Xavier M. T. et ai.: Chemical structures of a galactose-rich glycoprotein of Leishmania tarentolae. Compo
Biochem. Physiol. Pt. B 88: 101-104 (1987)
293. Yamasaki K.: Characterization and partial purification of a mannanlike polysaccharide in the eggs of
Locusta migratoria. Insect Biochem. 3: 79-90
(1973)
294. Yet M. G. and Wold E: The distribution of glycan
structures in individual N-glycosylation sites in animal
and plant glycoproteins. Arch. Biochem. Biophys.
278: 356-364 (1990)
295. Yokota K., Nishi Y. and Takesue Y.: Purification and
characterization of amphiphilic trehalase from rabbit
small intestine. Biochim. biophys. Acta 881: 405-414
(1986)
296. Zachary D. and Hoffmann D.: Lysozyme is stored in
the granules of certain haemocyte types in Locusta. J.
Insect Physiol. 30: 405-411 (1984)
297. Zera A. J., Koehn R. K. and Hall J. G.: Allozymes
and biological adaptation. In: Kerkut G. A. and Gilbert L. I. (eds.): Comprehensive insect physiology,
biochemistry and pharmacology, Vol. 10, pp.
633-674. Pergamon Press, Oxford 1985
298. Zhang W et al.: Primary structure of rabbit skeletal
muscle glycogen synthase deduced from cDNA clones. Faseb J. 3: 2532-36 (1989)
299. Zinkler D., Gotze M. and Fabian K.: Cellulose digestion in "primitive insects" (Apterygota) and oribatid
mites. Zool. Beitr. N. E 30: 17-28 (1986)