Isolation and characterization of a trypsin from the Slipper Lobster, Thenus orientalis(Lund)

Johnston, Danielle, Hermans, Josephine M., and Yellowlees, David (1995) Isolation and characterization of a trypsin from the Slipper Lobster, Thenus orientalis(Lund). Archives of Biochemistry and Biophysics, 324 (1). pp. 35-40.

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Trypsin has been isolated and purified from the digestive glands of the slipper lobster, Thenus orientalis. It is a glycoprotein with a molecular mass of approximately 35 kDa as judged by both SDS–PAGE and gel filtration. The N-terminal amino acid sequence has strong homology to crustacean trypsins. This is confirmed by the cross-reaction of crustacean trypsins with antibodies to the T. orientalisenzyme. Despite a 40% identity with the bovine trypsin N-terminal sequence, there was no cross-reaction with the mammalian serine proteases. The optimum k(cat) and k(cat)/K(m) values for N-α-benzoylarginine-p-nitroanalide were 0.91 s⁻¹and 9.7 × 103M⁻¹s⁻¹, respectively, with this specificity constant being lower than those reported for other crustacean trypsins. Inhibition studies indicated the presence of serine and histidine at the active site and pKₐ of the catalytic histidine residue was found to be 5.7 in the free enzyme and 4.7 in the Michaelis complex.

Item ID: 27307
Item Type: Article (Research - C1)
ISSN: 1096-0384
Date Deposited: 30 May 2013 04:14
FoR Codes: 06 BIOLOGICAL SCIENCES > 0603 Evolutionary Biology > 060399 Evolutionary Biology not elsewhere classified @ 33%
06 BIOLOGICAL SCIENCES > 0606 Physiology > 060603 Animal Physiology Systems @ 34%
06 BIOLOGICAL SCIENCES > 0608 Zoology > 060808 Invertebrate Biology @ 33%
SEO Codes: 96 ENVIRONMENT > 9608 Flora, Fauna and Biodiversity > 960899 Flora, Fauna and Biodiversity of Environments not elsewhere classified @ 49%
97 EXPANDING KNOWLEDGE > 970106 Expanding Knowledge in the Biological Sciences @ 51%
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