Canine haptoglobin: A unique haptoglobin subunit arrangement

Alexander Kurosky; Regine E. Hay; Barbara H. Bowman

doi:10.1016/0305-0491(79)90100-7

Canine haptoglobin: A unique haptoglobin subunit arrangement

Alexander Kurosky
, Regine E. Hay
, Barbara H. Bowman

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

16 Scopus citations

Abstract

1. 1. Isolated canine haptoglobin behaved identically to the α₂β₂ structure typical of human haptoglobin type 1-1 on alkaline polyacrylamide gel electrophoresis and on gel filtration. 2. 2. In the presence of urea or sodium dodecyl sulphate canine haptoglobin dissociated into αβ subunits that separated into α and β chains after reduction with 2-mercaptoethanol. 3. 3. Compositional analysis identified one less half-cystine in canine α chain when compared to human α¹ chain. 4. 4. These results provide evidence that there is no inter α chain disulphide in canine haptoglobin comparable to the α¹20-α¹20 disulphide in human haptoglobin that links the two αβ subunits.

Original language	English (US)
Pages (from-to)	339-344
Number of pages	6
Journal	Comparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume	62
Issue number	4
DOIs	https://doi.org/10.1016/0305-0491(79)90100-7
State	Published - 1979
Externally published	Yes

ASJC Scopus subject areas

Aquatic Science
Animal Science and Zoology
Molecular Biology
Biochemistry
Physiology

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10.1016/0305-0491(79)90100-7

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@article{58156273b9b645faa590911142c314c7,

title = "Canine haptoglobin: A unique haptoglobin subunit arrangement",

abstract = "1. 1. Isolated canine haptoglobin behaved identically to the α2β2 structure typical of human haptoglobin type 1-1 on alkaline polyacrylamide gel electrophoresis and on gel filtration. 2. 2. In the presence of urea or sodium dodecyl sulphate canine haptoglobin dissociated into αβ subunits that separated into α and β chains after reduction with 2-mercaptoethanol. 3. 3. Compositional analysis identified one less half-cystine in canine α chain when compared to human α1 chain. 4. 4. These results provide evidence that there is no inter α chain disulphide in canine haptoglobin comparable to the α120-α120 disulphide in human haptoglobin that links the two αβ subunits.",

author = "Alexander Kurosky and Hay, \{Regine E.\} and Bowman, \{Barbara H.\}",

note = "Funding Information: In all species investigated that possess nonpoly-meric Hp, the functional molecule is a tetrachain structure comprised of two \textasciitilde{}t and two fl chains that are covalently linked by interchain disulphide bonds (Smithies et al., 1962a; Malchy \& Dixon, 1973a; Malchy et al., 1973; Kurosky et al., 1976a; Shim et al., 1971; Lockhart et al., 1972; Shim et al., 1975; Kong \& Shim, 1974). A single disulphide bridge attaches the \textasciitilde{}t and fl chains to form an 0\textasciitilde{}fl subunit in human Hp 1-1. Two such subunits are combined by an ct120-ct120 disulphide bond (Malchy \& Dixon, 1973a; Kurosky et al., 1976a). The structure of human * This investigation was supported by grant HD 03321 from the National Institute of Child Health and Human Development. t To whom correspondence should be addressed. § Abbreviations: Hp, haptoglobin (intact); hp, haptoglobin (chains); Hb, hemoglobin; Pth, phenylthiohydantoin; SDS, sodium dodecyl sulphate; EDTA, ethylenediaminetetracetic acid. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",

year = "1979",

doi = "10.1016/0305-0491(79)90100-7",

language = "English (US)",

volume = "62",

pages = "339--344",

journal = "Comparative Biochemistry and Physiology -- Part B: Biochemistry and",

issn = "0305-0491",

publisher = "Elsevier B.V.",

number = "4",

}

TY - JOUR

T1 - Canine haptoglobin

T2 - A unique haptoglobin subunit arrangement

AU - Kurosky, Alexander

AU - Hay, Regine E.

AU - Bowman, Barbara H.

N1 - Funding Information: In all species investigated that possess nonpoly-meric Hp, the functional molecule is a tetrachain structure comprised of two ~t and two fl chains that are covalently linked by interchain disulphide bonds (Smithies et al., 1962a; Malchy & Dixon, 1973a; Malchy et al., 1973; Kurosky et al., 1976a; Shim et al., 1971; Lockhart et al., 1972; Shim et al., 1975; Kong & Shim, 1974). A single disulphide bridge attaches the ~t and fl chains to form an 0~fl subunit in human Hp 1-1. Two such subunits are combined by an ct120-ct120 disulphide bond (Malchy & Dixon, 1973a; Kurosky et al., 1976a). The structure of human * This investigation was supported by grant HD 03321 from the National Institute of Child Health and Human Development. t To whom correspondence should be addressed. § Abbreviations: Hp, haptoglobin (intact); hp, haptoglobin (chains); Hb, hemoglobin; Pth, phenylthiohydantoin; SDS, sodium dodecyl sulphate; EDTA, ethylenediaminetetracetic acid. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.

PY - 1979

Y1 - 1979

N2 - 1. 1. Isolated canine haptoglobin behaved identically to the α2β2 structure typical of human haptoglobin type 1-1 on alkaline polyacrylamide gel electrophoresis and on gel filtration. 2. 2. In the presence of urea or sodium dodecyl sulphate canine haptoglobin dissociated into αβ subunits that separated into α and β chains after reduction with 2-mercaptoethanol. 3. 3. Compositional analysis identified one less half-cystine in canine α chain when compared to human α1 chain. 4. 4. These results provide evidence that there is no inter α chain disulphide in canine haptoglobin comparable to the α120-α120 disulphide in human haptoglobin that links the two αβ subunits.

AB - 1. 1. Isolated canine haptoglobin behaved identically to the α2β2 structure typical of human haptoglobin type 1-1 on alkaline polyacrylamide gel electrophoresis and on gel filtration. 2. 2. In the presence of urea or sodium dodecyl sulphate canine haptoglobin dissociated into αβ subunits that separated into α and β chains after reduction with 2-mercaptoethanol. 3. 3. Compositional analysis identified one less half-cystine in canine α chain when compared to human α1 chain. 4. 4. These results provide evidence that there is no inter α chain disulphide in canine haptoglobin comparable to the α120-α120 disulphide in human haptoglobin that links the two αβ subunits.

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U2 - 10.1016/0305-0491(79)90100-7

DO - 10.1016/0305-0491(79)90100-7

M3 - Article

C2 - 318449

AN - SCOPUS:0018349716

SN - 0305-0491

VL - 62

SP - 339

EP - 344

JO - Comparative Biochemistry and Physiology -- Part B: Biochemistry and

JF - Comparative Biochemistry and Physiology -- Part B: Biochemistry and

IS - 4

ER -

Canine haptoglobin: A unique haptoglobin subunit arrangement

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