title: Hydrolases of Hysterothylacium aduncum (Nematoda).
abstract: BACKGROUND
  Enzymatic activity is an indicator of an organism's metabolic rate which depends on, i.e., environmental conditions, developmental stage, physiological stage, and sex. The API ZYM test was applied to compare activities of 19 hydrolases of female and male Hysterothylacium aduncum.
  
  
  METHODS
  Sexually mature nematodes were isolated from eelpout individuals caught in the Gulf of Gdańsk. Enzymatic activity of the hydrolases and the protein content was determined in nematode extracts using API ZYM and Bradford's method, respectively.
  
  
  RESULTS
  The females and males tested showed a total of 13 enzymes to be active. The males showed additionally the presence of alpha-fucosidase. Acidic and alkaline phosphatases had very high activities in both sexes; short-chain fatty acid esterases, leucine and valine aminopeptidases, alpha-glucosidase, and N-acetylglucosaminidase were highly active. H. aduncum showed no trypsin- and chymotrypsin-specific activities; similarly, no activity of alpha-galactosidase, alpha-mannosidase, and beta-glucuronidase was revealed. Except for lipase (C14), hydrolases were more active in females than in males, which is related to metabolic rate being higher in females due to their reproductive function.
  
  
  CONCLUSIONS
  Comparison of the results obtained with earlier data produced with API ZYM allowed suggesting that the hydrolase pattern may be more affected by habitat in the host than by the taxonomic affiliation of nematode.
authors.affiliation: Department of Biochemistry, Faculty of Biology, University of Warmia and Mazury, Oczapowskiego 1A, 10-719 Olsztyn, Poland. k.zoltowska@uwm.edu.pl
authors.forename: Krystyna
authors.initials: K
authors.lastname: Zółtowska
authors.forename: Małgorzata
authors.initials: M
authors.lastname: Dmitryjuk
authors.forename: Jerzy
authors.initials: J
authors.lastname: Rokicki
authors.forename: Elzbieta
authors.initials: E
authors.lastname: Lopieńska-Biernat
mesh_terms: D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D004950:Esterases / Q000378:metabolism; D005260:Female; D005399:Fishes / Q000469:parasitology; D006026:Glycoside Hydrolases / Q000378:metabolism; D006867:Hydrolases / Q000378:metabolism*; D007814:Larva / Q000201:enzymology; D008049:Lipase / Q000378:metabolism; D008297:Male; D009348:Nematoda / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000378:metabolism; D011044:Poland; D012737:Sex Factors; D000520:alpha-Glucosidases / Q000378:metabolism; D001616:beta-Galactosidase / Q000378:metabolism; D001617:beta-Glucosidase / Q000378:metabolism
chemical_list: D006867:Hydrolases; D004950:Esterases; D008049:Lipase; D000469:Alkaline Phosphatase; D006026:Glycoside Hydrolases; D000520:alpha-Glucosidases; D001617:beta-Glucosidase; D001616:beta-Galactosidase; D010447:Peptide Hydrolases