Isolation and characterization of two cDNAs from Atlantic cod encoding two distinct psychrophilic elastases

Elín Gudmundsdóttir; Rémi Spilliaert; Qing Yang; Charles S. Craik; Jón B. Bjarnason; Águsta Gudmundsdóttir

doi:10.1016/0305-0491(95)02109-4

Isolation and characterization of two cDNAs from Atlantic cod encoding two distinct psychrophilic elastases

Elín Gudmundsdóttir, Rémi Spilliaert, Qing Yang, Charles S. Craik, Jón B. Bjarnason, Águsta Gudmundsdóttir

Faculty of Food Science and Nutrition

University of Iceland

Research output: Contribution to journal › Article › peer-review

Abstract

The cDNAs encoding two different Atlantic cod elastases have been isolated and sequenced. The predicted amino acid sequences revealed two preproelastases, consisting of a signal peptide, an activation peptide and a mature enzyme of 242 and 239 amino acids. Amino acid sequence identity between the two cod elastases was 60.1% and identity with mammalian elastases ranged from 50-64%. The two cod elastases contain all the major structural features common to serine proteases, such as the catalytic triad His57, Asp102 and Ser195. Both cod elastases have a high content of methionine, consistent with previous findings in psychrophilic fish enzymes.

Original language	English
Pages (from-to)	795-801
Number of pages	7
Journal	Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume	113
Issue number	4
DOIs	https://doi.org/10.1016/0305-0491(95)02109-4
Publication status	Published - 1996

Other keywords

Atlantic cod
cDNA sequence
elastase
psychrophilic
serine protease

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10.1016/0305-0491(95)02109-4

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title = "Isolation and characterization of two cDNAs from Atlantic cod encoding two distinct psychrophilic elastases",

abstract = "The cDNAs encoding two different Atlantic cod elastases have been isolated and sequenced. The predicted amino acid sequences revealed two preproelastases, consisting of a signal peptide, an activation peptide and a mature enzyme of 242 and 239 amino acids. Amino acid sequence identity between the two cod elastases was 60.1\% and identity with mammalian elastases ranged from 50-64\%. The two cod elastases contain all the major structural features common to serine proteases, such as the catalytic triad His57, Asp102 and Ser195. Both cod elastases have a high content of methionine, consistent with previous findings in psychrophilic fish enzymes.",

keywords = "Atlantic cod, cDNA sequence, elastase, psychrophilic, serine protease",

author = "El{\'i}n Gudmundsd{\'o}ttir and R{\'e}mi Spilliaert and Qing Yang and Craik, \{Charles S.\} and Bjarnason, \{J{\'o}n B.\} and {\'A}gusta Gudmundsd{\'o}ttir",

year = "1996",

doi = "10.1016/0305-0491(95)02109-4",

language = "English",

volume = "113",

pages = "795--801",

journal = "Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology",

issn = "0305-0491",

publisher = "Elsevier Inc.",

number = "4",

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TY - JOUR

T1 - Isolation and characterization of two cDNAs from Atlantic cod encoding two distinct psychrophilic elastases

AU - Gudmundsdóttir, Elín

AU - Spilliaert, Rémi

AU - Yang, Qing

AU - Craik, Charles S.

AU - Bjarnason, Jón B.

AU - Gudmundsdóttir, Águsta

PY - 1996

Y1 - 1996

N2 - The cDNAs encoding two different Atlantic cod elastases have been isolated and sequenced. The predicted amino acid sequences revealed two preproelastases, consisting of a signal peptide, an activation peptide and a mature enzyme of 242 and 239 amino acids. Amino acid sequence identity between the two cod elastases was 60.1% and identity with mammalian elastases ranged from 50-64%. The two cod elastases contain all the major structural features common to serine proteases, such as the catalytic triad His57, Asp102 and Ser195. Both cod elastases have a high content of methionine, consistent with previous findings in psychrophilic fish enzymes.

AB - The cDNAs encoding two different Atlantic cod elastases have been isolated and sequenced. The predicted amino acid sequences revealed two preproelastases, consisting of a signal peptide, an activation peptide and a mature enzyme of 242 and 239 amino acids. Amino acid sequence identity between the two cod elastases was 60.1% and identity with mammalian elastases ranged from 50-64%. The two cod elastases contain all the major structural features common to serine proteases, such as the catalytic triad His57, Asp102 and Ser195. Both cod elastases have a high content of methionine, consistent with previous findings in psychrophilic fish enzymes.

KW - Atlantic cod

KW - cDNA sequence

KW - elastase

KW - psychrophilic

KW - serine protease

UR - https://www.scopus.com/pages/publications/0029948899

U2 - 10.1016/0305-0491(95)02109-4

DO - 10.1016/0305-0491(95)02109-4

M3 - Article

C2 - 8925447

SN - 0305-0491

VL - 113

SP - 795

EP - 801

JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

IS - 4

ER -

Isolation and characterization of two cDNAs from Atlantic cod encoding two distinct psychrophilic elastases

Abstract

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