Cold-adapted structural properties of trypsins from walleye pollock (Theragra chalcogramma) and Arctic cod (Boreogadus saida)

Kanno, Gaku; Kishimura, Hideki; Yamamoto, Jun; Ando, Seiichi; Shimizu, Takeshi; Benjakul, Soottawat; Klomklao, Sappasith; Nalinanon, Sitthipong; Chun, Byung‐Soo; Saeki, Hiroki

doi:10.1007/s00217-011-1592-8

Cited by 6 publications

(2 citation statements)

References 41 publications

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“…Generally, fish trypsins had a charged Glu residue at position 6, where Thr is most common in mammalian pancreatic trypsins. Moreover, the sequence of all trypsins started with IVGG after limited proteolysis of inactive trypsinogen into the active trypsin form (Kanno et al, 2010(Kanno et al, , 2011a2011b).…”

Section: Trypsins N-terminal Sequences Alignmentmentioning

confidence: 99%

Trypsins from fish processing waste: characteristics and biotechnological applications – comprehensive review

Bougatef

2013

Journal of Cleaner Production

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Section: Trypsins N-terminal Sequences Alignmentmentioning

confidence: 99%

Trypsins from fish processing waste: characteristics and biotechnological applications – comprehensive review

Bougatef

2013

Journal of Cleaner Production

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“…Briefly,Shimizu et al 13 the forward primer (5'-CCCTGTTCTCTGCCATTTGA-3') was designed upstream of the coding to the N-terminal amino acid sequence of '-c, and the reverse primer (5'-CTGGGTGCTTCCTTCTGATA-3') was designed downstream from the sequence encoding the 170th amino acid residue in order to cover the whole amino acid sequence of the 18kDa-subunit. cDNA cloning was carried out as described previously(24), with the exception of primer differences. The nucleotide sequence was determined using theDNA Sequencer 3130 (Life Technologies, Carlsbad, CA) after labeling the DNA with the BigDye Terminator v3.1 Cycle Sequencing Kit (Life Technologies).…”

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confidence: 99%

Molecular and immunological characterization of β′-component (Onc k 5), a major IgE-binding protein in chum salmon roe

Shimizu

Kishimura

Kanno

et al. 2013

International Immunology

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Salmon roe has a high allergic potency and often causes anaphylaxis in Japan. The major allergic protein of salmon roe is β'-component, which is a 35kDa vitellogenin fragment consisting of two subunits. To elucidate structural information and immunological characteristics, β'-component and the subunit components were purified from chum salmon (Onchorhincus keta) roe and vitellogenin-encoding mRNA was used to prepare β'-component subunit-encoding cDNA. This was PCR-amplified, cloned and sequenced and the deduced amino acid sequence compared with partial sequences of β'-component obtained by peptide mapping. The recombinant β'-component subunit was produced by bacterial expression in Escherichia coli and its IgE-binding ability was measured by ELISA using the sera of a patient allergic to salmon roe. This was then compared with that of the native β'-component with and without carboxymethylation. Following successful cloning of the cDNA encoding the β'-component subunit, 170 amino acid residues were deduced and matched with the amino acid sequences of 121 and 88 residues in the 16kDa and 18kDa subunits, respectively. The sequences of both β'-component subunits were almost identical, and the predicted secondary structure of the β'-component showed a high content of β-pleated sheets and no α-helices. There was no difference in IgE-binding ability between the native and recombinant β'-component subunits at the same protein concentration, regardless of carboxymethylation. In conclusion, β'-component is a homodimer protein composed of two isoform subunits having the same level of IgE-binding ability and, therefore, allergenic identity.

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A thermostable trypsin from freshwater fish Japanese dace (Tribolodon hakonensis): a comparison of the primary structures among fish trypsins

Kanno

Klomklao

Kumagai

et al. 2018

Fish Physiol Biochem

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Trypsin from Japanese dace (Tribolodon hakonensis) (JD-T) living in freshwater (2-18 o C) was purified. JD-T represented typical fish trypsin characteristics regarding the effects of protease inhibitor, calcium-ion and pH. For the effect of temperature, JD-T quite resembled to the trypsins from tropical-zone marine fish and freshwater fish (the catfish cultured in Thailand), i.e., the optimum temperature was 60 °C, and it was stable below 60 °C at pH 8.0 for 15 min incubation. From the data, it seemed that the trypsin from freshwater fish is thermostable in spite of the fact that their habitat temperatures are low. So, we determined the primary structure of JD-T to discuss its thermostability-structure relationship. JD-T possessed basic structural features of fish trypsin such as the catalytic triad, the Asp189 residue for substrate specificity, twelve Cys residues forming six disulfide-bridges, and the calcium-ion-binding loop. On the other hand, the contents of charged amino acid residues in whole JD-T molecule (16.2 %) and N-terminal region (13.8 %) were similar to those of tropical-zone marine fish and other freshwater fish trypsins. Then, JD-T conserved the five amino acid residues (Glu70, Asn72, Val75, Glu77 and Glu80) coordinate with calcium-ion, and the proportion of negatively charged amino acids to charged amino acids in the calcium-ion-binding region of JD-T (75.0 %) was equivalent to those of tropical-zone marine fish and freshwater fish trypsins. Therefore, it was suggested that the high thermostability of JD-T are stemmed from these structural specificities.

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Cold-adapted structural properties of trypsins from walleye pollock (Theragra chalcogramma) and Arctic cod (Boreogadus saida)

Cited by 6 publications

References 41 publications

Trypsins from fish processing waste: characteristics and biotechnological applications – comprehensive review

Trypsins from fish processing waste: characteristics and biotechnological applications – comprehensive review

Molecular and immunological characterization of β′-component (Onc k 5), a major IgE-binding protein in chum salmon roe

A thermostable trypsin from freshwater fish Japanese dace (Tribolodon hakonensis): a comparison of the primary structures among fish trypsins

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