The primary structure of myoglobin from yellowfin tuna (Thunnus albacares).

D. A. Watts, R. H. Rice, W. D. Brown

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

The amino acid sequence of myoglobin from yellowfin tuna (Thunnus albacares) has been determined. The globin is an aminoacetylated chain containing 146 residues and having deletions, with respect to mammalian and avian myoglobins, at the NH2 terminus and two internal locations. From 79 to 85 amino acid substitutions are observed between this myoglobin and those of mammals, birds, and shark. Two external regions containing 6 and 7 residues, which are highly conserved in mammalian and avian myoglobins, are greatly or totally altered in the tuna sequence. Significant differences are apparent in the extent of electrostatic bonding in the myoglobins of fish and in those of mammals or birds.

Original languageEnglish (US)
Pages (from-to)10916-10924
Number of pages9
JournalJournal of Biological Chemistry
Volume255
Issue number22
StatePublished - Nov 25 1980
Externally publishedYes

Fingerprint

Myoglobin
Mammals
Birds
Amino Acids
Sharks
Globins
Amino Acid Substitution
Static Electricity
Fish
Amino Acid Sequence
Electrostatics
Fishes
Substitution reactions

ASJC Scopus subject areas

  • Biochemistry

Cite this

Watts, D. A., Rice, R. H., & Brown, W. D. (1980). The primary structure of myoglobin from yellowfin tuna (Thunnus albacares). Journal of Biological Chemistry, 255(22), 10916-10924.

The primary structure of myoglobin from yellowfin tuna (Thunnus albacares). / Watts, D. A.; Rice, R. H.; Brown, W. D.

In: Journal of Biological Chemistry, Vol. 255, No. 22, 25.11.1980, p. 10916-10924.

Research output: Contribution to journalArticle

Watts, DA, Rice, RH & Brown, WD 1980, 'The primary structure of myoglobin from yellowfin tuna (Thunnus albacares).', Journal of Biological Chemistry, vol. 255, no. 22, pp. 10916-10924.
Watts, D. A. ; Rice, R. H. ; Brown, W. D. / The primary structure of myoglobin from yellowfin tuna (Thunnus albacares). In: Journal of Biological Chemistry. 1980 ; Vol. 255, No. 22. pp. 10916-10924.
@article{96a26f13b59e4b3eb74ccbc146e5fd7f,
title = "The primary structure of myoglobin from yellowfin tuna (Thunnus albacares).",
abstract = "The amino acid sequence of myoglobin from yellowfin tuna (Thunnus albacares) has been determined. The globin is an aminoacetylated chain containing 146 residues and having deletions, with respect to mammalian and avian myoglobins, at the NH2 terminus and two internal locations. From 79 to 85 amino acid substitutions are observed between this myoglobin and those of mammals, birds, and shark. Two external regions containing 6 and 7 residues, which are highly conserved in mammalian and avian myoglobins, are greatly or totally altered in the tuna sequence. Significant differences are apparent in the extent of electrostatic bonding in the myoglobins of fish and in those of mammals or birds.",
author = "Watts, {D. A.} and Rice, {R. H.} and Brown, {W. D.}",
year = "1980",
month = "11",
day = "25",
language = "English (US)",
volume = "255",
pages = "10916--10924",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "22",

}

TY - JOUR

T1 - The primary structure of myoglobin from yellowfin tuna (Thunnus albacares).

AU - Watts, D. A.

AU - Rice, R. H.

AU - Brown, W. D.

PY - 1980/11/25

Y1 - 1980/11/25

N2 - The amino acid sequence of myoglobin from yellowfin tuna (Thunnus albacares) has been determined. The globin is an aminoacetylated chain containing 146 residues and having deletions, with respect to mammalian and avian myoglobins, at the NH2 terminus and two internal locations. From 79 to 85 amino acid substitutions are observed between this myoglobin and those of mammals, birds, and shark. Two external regions containing 6 and 7 residues, which are highly conserved in mammalian and avian myoglobins, are greatly or totally altered in the tuna sequence. Significant differences are apparent in the extent of electrostatic bonding in the myoglobins of fish and in those of mammals or birds.

AB - The amino acid sequence of myoglobin from yellowfin tuna (Thunnus albacares) has been determined. The globin is an aminoacetylated chain containing 146 residues and having deletions, with respect to mammalian and avian myoglobins, at the NH2 terminus and two internal locations. From 79 to 85 amino acid substitutions are observed between this myoglobin and those of mammals, birds, and shark. Two external regions containing 6 and 7 residues, which are highly conserved in mammalian and avian myoglobins, are greatly or totally altered in the tuna sequence. Significant differences are apparent in the extent of electrostatic bonding in the myoglobins of fish and in those of mammals or birds.

UR - http://www.scopus.com/inward/record.url?scp=0019333181&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0019333181&partnerID=8YFLogxK

M3 - Article

C2 - 7430163

AN - SCOPUS:0019333181

VL - 255

SP - 10916

EP - 10924

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 22

ER -