Disulphide bridges of bovine factor X

P Højrup, S Magnusson

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Evidence is presented for the disulphide bridges in bovine Factor X. The protein was degraded by chemical and enzymic means, and all 12 disulphide bridges were isolated in separate peptides except for bridges nos. 6/7 in the light chain. All the disulphide bridges were found to be in positions corresponding to those found in other homologous domains. This report is the first verification of an epidermal-growth-factor-homologous domain having the same disulphide-bonding pattern as that found in mouse epidermal growth factor.

OriginalsprogEngelsk
TidsskriftThe Biochemical journal
Vol/bind245
Udgave nummer3
Sider (fra-til)887-91
Antal sider5
ISSN0264-6021
DOI
StatusUdgivet - 1. aug. 1987

Fingeraftryk

Factor X
Disulfides
Epidermal Growth Factor
Peptides
Proteins

Citer dette

Højrup, P ; Magnusson, S. / Disulphide bridges of bovine factor X. I: The Biochemical journal. 1987 ; Bind 245, Nr. 3. s. 887-91.
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Disulphide bridges of bovine factor X. / Højrup, P; Magnusson, S.

I: The Biochemical journal, Bind 245, Nr. 3, 01.08.1987, s. 887-91.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Disulphide bridges of bovine factor X

AU - Højrup, P

AU - Magnusson, S

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N2 - Evidence is presented for the disulphide bridges in bovine Factor X. The protein was degraded by chemical and enzymic means, and all 12 disulphide bridges were isolated in separate peptides except for bridges nos. 6/7 in the light chain. All the disulphide bridges were found to be in positions corresponding to those found in other homologous domains. This report is the first verification of an epidermal-growth-factor-homologous domain having the same disulphide-bonding pattern as that found in mouse epidermal growth factor.

AB - Evidence is presented for the disulphide bridges in bovine Factor X. The protein was degraded by chemical and enzymic means, and all 12 disulphide bridges were isolated in separate peptides except for bridges nos. 6/7 in the light chain. All the disulphide bridges were found to be in positions corresponding to those found in other homologous domains. This report is the first verification of an epidermal-growth-factor-homologous domain having the same disulphide-bonding pattern as that found in mouse epidermal growth factor.

KW - Amino Acids/analysis

KW - Animals

KW - Cattle

KW - Disulfides/analysis

KW - Factor X

KW - Peptide Fragments/analysis

U2 - 10.1042/bj2450887

DO - 10.1042/bj2450887

M3 - Journal article

C2 - 3663198

VL - 245

SP - 887

EP - 891

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

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