Primary structure of turkey myoglobin

被引：13

作者：

Joseph, Poulson ^{[1
]}

Suman, Surendranath P. ^{[1
]}

Li, Shuting ^{[1
]}

Claus, James R. ^{[2
]}

Fontaine, Michele ^{[3
]}

Steinke, Laurey ^{[3
]}

机构：

[1] Univ Kentucky, Dept Anim & Food Sci, Lexington, KY 40546 USA

[2] Univ Wisconsin, Meat Sci & Muscle Biol Lab, Madison, WI 53706 USA

[3] Univ Nebraska Med Ctr, Prot Struct Core Facil, Omaha, NE 68198 USA

来源：

FOOD CHEMISTRY | 2011年 / 129卷 / 01期

关键词：

Turkey; Meleagris gallopavo; Myoglobin; Primary structure; Edman degradation; PINK COLOR DEFECT; CHICKEN BREAST MEAT; CARBON-MONOXIDE; TUNA MYOGLOBIN; COOKED BEEF; SEQUENCE; THERMOSTABILITY; PROTEINS; PORCINE; PH;

D O I：

10.1016/j.foodchem.2011.04.024

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

Our objective was to determine the amino acid sequence of turkey myoglobin. Turkey myoglobin was isolated from cardiac muscles via ammonium sulphate precipitation and gel-filtration chromatography. Purified turkey myoglobin, separated as a 17 kDa band in SDS-PAGE, was subjected to digestion with trypsin or aspartic acid endopeptidase. The resulting peptides were separated by reverse-phase HPLC, and then subjected to Edman degradation to obtain the amino acid sequence. The complete amino acid sequence of turkey myoglobin was determined and compared with that of poultry and red meat myoglobins. Turkey myoglobin has 153 amino acids and nine histidine residues. Proximal (position 93) and distal (position 64) histidine residues, responsible for maintaining the stability of haeme, are conserved in turkey myoglobin. Turkey myoglobin shares 100% sequence similarity with chicken myoglobin, whereas it shares 92.5% homology with ostrich, 76.5% with pig, and less than 73% with ruminant myoglobins. (C) 2011 Elsevier Ltd. All rights reserved.

引用

页码：175 / 178

页数：4

共 29 条

[1] ROLE OF REDUCED HEMOCHROMES IN PINK COLOR DEFECT OF COOKED TURKEY ROLLS [J].

CORNFORTH, DP ;

VAHABZADEH, F ;

CARPENTER, CE ;

BARTHOLOMEW, DT .

JOURNAL OF FOOD SCIENCE, 1986, 51 (05) :1132-1135

[2] Carbon monoxide, nitric oxide, and nitrogen dioxide levels in gas ovens related to surface pinking of cooked beef and turkey [J].

Cornforth, DP ;

Rabovitser, JK ;

Ahuja, S ;

Wagner, JC ;

Hanson, R ;

Cummings, B ;

Chudnovsky, Y .

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1998, 46 (01) :255-261

[3] ISOLATION AND PURIFICATION OF TURKEY HEME PROTEINS [J].

CORNISH, DG ;

FRONING, GW .

POULTRY SCIENCE, 1974, 53 (01) :365-377

[4] PRIMARY SEQUENCE OF CHICKEN MYOGLOBIN (GALLUS-GALLUS) [J].

DECONINCK, M ;

PEIFFER, S ;

DEPRETER, J ;

PAUL, C ;

SCHENK, AG ;

LEONIS, J .

BIOCHIMICA ET BIOPHYSICA ACTA, 1975, 386 (02) :567-575

[5] Characterization and kinetics studies of water buffalo (Bubalus bubalis) myoglobin [J].

Dosi, Roberta ;

Di Maro, Antirno ;

Chambery, Angela ;

Colonna, Giovanni ;

Costantini, Susan ;

Geraci, Giuseppe ;

Parente, Augusto .

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 2006, 145 (02) :230-238

[6]

EDMAN P, 1949, ARCH BIOCHEM, V22, P475

[7] Primary structure of myoglobins from 31 species of birds [J].

Enoki, Yasunori ;

Ohga, Yoshimi ;

Ishidate, Hiromi ;

Morimoto, Tomotoshi .

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 2008, 149 (01) :11-21

[8]

Holownia K, 2004, J FOOD SCI, V69, pC194

[9] Evaluation of induced color changes in chicken breast meat during simulation of pink color defect [J].

Holownia, K ;

Chinnan, MS ;

Reynolds, AE ;

Koehler, PE .

POULTRY SCIENCE, 2003, 82 (06) :1049-1059

[10] Pink color defect in poultry white meat as affected by endogenous conditions [J].

Holownia, K ;

Chinnan, MS ;

Reynolds, AE .

JOURNAL OF FOOD SCIENCE, 2003, 68 (03) :742-747

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