Amino acid sequence of myoglobin from white-tailed deer (Odocoileus virginianus)

Poulson Joseph, Surendranath P. Suman, Shuting Li, Michele Fontaine, Laurey A Steinke

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Our objective was to determine the primary structure of white-tailed deer myoglobin (Mb). White-tailed deer Mb was isolated from cardiac muscles employing ammonium sulfate precipitation and gel-filtration chromatography. The amino acid sequence was determined by Edman degradation. Sequence analyses of intact Mb as well as tryptic- and cyanogen bromide-peptides yielded the complete primary structure of white-tailed deer Mb, which shared 100% similarity with red deer Mb. White-tailed deer Mb consists of 153 amino acid residues and shares more than 96% sequence similarity with myoglobins from meat-producing ruminants, such as cattle, buffalo, sheep, and goat. Similar to sheep and goat myoglobins, white-tailed deer Mb contains 12 histidine residues. Proximal (position 93) and distal (position 64) histidine residues responsible for maintaining the stability of heme are conserved in white-tailed deer Mb.

Original languageEnglish (US)
Pages (from-to)160-163
Number of pages4
JournalMeat Science
Volume92
Issue number2
DOIs
StatePublished - Oct 1 2012

Fingerprint

Deer
myoglobin
Myoglobin
Odocoileus virginianus
Amino Acid Sequence
amino acid sequences
histidine
Histidine
Goats
Sheep
goats
cyanogen
sheep
Cyanogen Bromide
Buffaloes
Ammonium Sulfate
Ruminants
heme
Cervus elaphus
myocardium

Keywords

  • Edman degradation
  • Myoglobin
  • Odocoileus virginianus
  • Primary structure
  • White-tailed deer

ASJC Scopus subject areas

  • Food Science

Cite this

Amino acid sequence of myoglobin from white-tailed deer (Odocoileus virginianus). / Joseph, Poulson; Suman, Surendranath P.; Li, Shuting; Fontaine, Michele; Steinke, Laurey A.

In: Meat Science, Vol. 92, No. 2, 01.10.2012, p. 160-163.

Research output: Contribution to journalArticle

Joseph, Poulson ; Suman, Surendranath P. ; Li, Shuting ; Fontaine, Michele ; Steinke, Laurey A. / Amino acid sequence of myoglobin from white-tailed deer (Odocoileus virginianus). In: Meat Science. 2012 ; Vol. 92, No. 2. pp. 160-163.
@article{c40b35c0b7974dee9c635375a67856a1,
title = "Amino acid sequence of myoglobin from white-tailed deer (Odocoileus virginianus)",
abstract = "Our objective was to determine the primary structure of white-tailed deer myoglobin (Mb). White-tailed deer Mb was isolated from cardiac muscles employing ammonium sulfate precipitation and gel-filtration chromatography. The amino acid sequence was determined by Edman degradation. Sequence analyses of intact Mb as well as tryptic- and cyanogen bromide-peptides yielded the complete primary structure of white-tailed deer Mb, which shared 100{\%} similarity with red deer Mb. White-tailed deer Mb consists of 153 amino acid residues and shares more than 96{\%} sequence similarity with myoglobins from meat-producing ruminants, such as cattle, buffalo, sheep, and goat. Similar to sheep and goat myoglobins, white-tailed deer Mb contains 12 histidine residues. Proximal (position 93) and distal (position 64) histidine residues responsible for maintaining the stability of heme are conserved in white-tailed deer Mb.",
keywords = "Edman degradation, Myoglobin, Odocoileus virginianus, Primary structure, White-tailed deer",
author = "Poulson Joseph and Suman, {Surendranath P.} and Shuting Li and Michele Fontaine and Steinke, {Laurey A}",
year = "2012",
month = "10",
day = "1",
doi = "10.1016/j.meatsci.2012.04.012",
language = "English (US)",
volume = "92",
pages = "160--163",
journal = "Meat Science",
issn = "0309-1740",
publisher = "Elsevier BV",
number = "2",

}

TY - JOUR

T1 - Amino acid sequence of myoglobin from white-tailed deer (Odocoileus virginianus)

AU - Joseph, Poulson

AU - Suman, Surendranath P.

AU - Li, Shuting

AU - Fontaine, Michele

AU - Steinke, Laurey A

PY - 2012/10/1

Y1 - 2012/10/1

N2 - Our objective was to determine the primary structure of white-tailed deer myoglobin (Mb). White-tailed deer Mb was isolated from cardiac muscles employing ammonium sulfate precipitation and gel-filtration chromatography. The amino acid sequence was determined by Edman degradation. Sequence analyses of intact Mb as well as tryptic- and cyanogen bromide-peptides yielded the complete primary structure of white-tailed deer Mb, which shared 100% similarity with red deer Mb. White-tailed deer Mb consists of 153 amino acid residues and shares more than 96% sequence similarity with myoglobins from meat-producing ruminants, such as cattle, buffalo, sheep, and goat. Similar to sheep and goat myoglobins, white-tailed deer Mb contains 12 histidine residues. Proximal (position 93) and distal (position 64) histidine residues responsible for maintaining the stability of heme are conserved in white-tailed deer Mb.

AB - Our objective was to determine the primary structure of white-tailed deer myoglobin (Mb). White-tailed deer Mb was isolated from cardiac muscles employing ammonium sulfate precipitation and gel-filtration chromatography. The amino acid sequence was determined by Edman degradation. Sequence analyses of intact Mb as well as tryptic- and cyanogen bromide-peptides yielded the complete primary structure of white-tailed deer Mb, which shared 100% similarity with red deer Mb. White-tailed deer Mb consists of 153 amino acid residues and shares more than 96% sequence similarity with myoglobins from meat-producing ruminants, such as cattle, buffalo, sheep, and goat. Similar to sheep and goat myoglobins, white-tailed deer Mb contains 12 histidine residues. Proximal (position 93) and distal (position 64) histidine residues responsible for maintaining the stability of heme are conserved in white-tailed deer Mb.

KW - Edman degradation

KW - Myoglobin

KW - Odocoileus virginianus

KW - Primary structure

KW - White-tailed deer

UR - http://www.scopus.com/inward/record.url?scp=84861966419&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84861966419&partnerID=8YFLogxK

U2 - 10.1016/j.meatsci.2012.04.012

DO - 10.1016/j.meatsci.2012.04.012

M3 - Article

C2 - 22608832

AN - SCOPUS:84861966419

VL - 92

SP - 160

EP - 163

JO - Meat Science

JF - Meat Science

SN - 0309-1740

IS - 2

ER -