Residues cys-1 and cys-79 are not essential for refolding of reduced-denatured kringle 4 fragment of human plasminogen

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Abstract

It was shown previously that the Cys-1-Cys-79 disulphide bond forms in the last step of refolding of kringle 4 and that this bond is not essential for the lysine-Sepharose affinity of the kringle 4 fragment (Trexler, M. and Patthy, L. (1983) Proc. Natl. Acad. Sci. U.S.A. 80 2457-2461). Here we show that kringle 4, carboxymethylated on Cys-1 and Cys-79, regains its lysine-Sepharose affinity following denaturation and reductive cleavage of its disulphide bonds. The rate of refolding under aerobic conditions or in the presence of oxidized and reduced glutathione was similar to that observed in the case of native kringle 4. Our results suggest that Cys-1 and Cys-79 residues of kringles are not essential for the maintenance or acquisition of the biologically active kringle-fold.

Original languageEnglish
Pages (from-to)275-280
Number of pages6
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume787
Issue number3
DOIs
Publication statusPublished - Jun 28 1984

Fingerprint

Kringles
Plasminogen
Disulfides
Regain
Denaturation
Glutathione Disulfide
Glutathione
lysine-sepharose
Maintenance

Keywords

  • (Human)
  • Cysteine residue
  • Kringle 4 fragment
  • Plasminogen
  • Protein refolding

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology
  • Medicine(all)

Cite this

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title = "Residues cys-1 and cys-79 are not essential for refolding of reduced-denatured kringle 4 fragment of human plasminogen",
abstract = "It was shown previously that the Cys-1-Cys-79 disulphide bond forms in the last step of refolding of kringle 4 and that this bond is not essential for the lysine-Sepharose affinity of the kringle 4 fragment (Trexler, M. and Patthy, L. (1983) Proc. Natl. Acad. Sci. U.S.A. 80 2457-2461). Here we show that kringle 4, carboxymethylated on Cys-1 and Cys-79, regains its lysine-Sepharose affinity following denaturation and reductive cleavage of its disulphide bonds. The rate of refolding under aerobic conditions or in the presence of oxidized and reduced glutathione was similar to that observed in the case of native kringle 4. Our results suggest that Cys-1 and Cys-79 residues of kringles are not essential for the maintenance or acquisition of the biologically active kringle-fold.",
keywords = "(Human), Cysteine residue, Kringle 4 fragment, Plasminogen, Protein refolding",
author = "M. Trexler and L. Patthy",
year = "1984",
month = "6",
day = "28",
doi = "10.1016/0167-4838(84)90320-0",
language = "English",
volume = "787",
pages = "275--280",
journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "3",

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T1 - Residues cys-1 and cys-79 are not essential for refolding of reduced-denatured kringle 4 fragment of human plasminogen

AU - Trexler, M.

AU - Patthy, L.

PY - 1984/6/28

Y1 - 1984/6/28

N2 - It was shown previously that the Cys-1-Cys-79 disulphide bond forms in the last step of refolding of kringle 4 and that this bond is not essential for the lysine-Sepharose affinity of the kringle 4 fragment (Trexler, M. and Patthy, L. (1983) Proc. Natl. Acad. Sci. U.S.A. 80 2457-2461). Here we show that kringle 4, carboxymethylated on Cys-1 and Cys-79, regains its lysine-Sepharose affinity following denaturation and reductive cleavage of its disulphide bonds. The rate of refolding under aerobic conditions or in the presence of oxidized and reduced glutathione was similar to that observed in the case of native kringle 4. Our results suggest that Cys-1 and Cys-79 residues of kringles are not essential for the maintenance or acquisition of the biologically active kringle-fold.

AB - It was shown previously that the Cys-1-Cys-79 disulphide bond forms in the last step of refolding of kringle 4 and that this bond is not essential for the lysine-Sepharose affinity of the kringle 4 fragment (Trexler, M. and Patthy, L. (1983) Proc. Natl. Acad. Sci. U.S.A. 80 2457-2461). Here we show that kringle 4, carboxymethylated on Cys-1 and Cys-79, regains its lysine-Sepharose affinity following denaturation and reductive cleavage of its disulphide bonds. The rate of refolding under aerobic conditions or in the presence of oxidized and reduced glutathione was similar to that observed in the case of native kringle 4. Our results suggest that Cys-1 and Cys-79 residues of kringles are not essential for the maintenance or acquisition of the biologically active kringle-fold.

KW - (Human)

KW - Cysteine residue

KW - Kringle 4 fragment

KW - Plasminogen

KW - Protein refolding

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U2 - 10.1016/0167-4838(84)90320-0

DO - 10.1016/0167-4838(84)90320-0

M3 - Article

C2 - 6329306

AN - SCOPUS:0021772396

VL - 787

SP - 275

EP - 280

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

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