Stopped-flow studies of the N ⇌ F transition in serum albumin

Ronald P. Taylor; Vincent Chau; Mathew J. Zenkowich; Luther H. Leake

doi:10.1016/0301-4622(78)85006-6

Stopped-flow studies of the N ⇌ F transition in serum albumin

Ronald P. Taylor, Vincent Chau, Mathew J. Zenkowich, Luther H. Leake

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

6 Scopus citations

Abstract

Stopped-flow studies of the refolding of iodoacetamide-blocked bovine serum albumin from the acid unfolded "F" state have been performed. If the protein is incubated with low concentrations of perchlorate anion then the refolding kinetics follow a simple first-order process. The dependence on pH of both the amplitude of the observed transients and the measured rate constants indicates that the N ⇌ F transition is highly cooperative. The results are consistent with the postulated multidomain structure of albumin which has been developed as a result of both sequence work and a variety of physical studies.

Original language	English (US)
Pages (from-to)	293-299
Number of pages	7
Journal	Biophysical Chemistry
Volume	7
Issue number	4
DOIs	https://doi.org/10.1016/0301-4622(78)85006-6
State	Published - Jan 1978

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Organic Chemistry

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10.1016/0301-4622(78)85006-6

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title = "Stopped-flow studies of the N ⇌ F transition in serum albumin",

abstract = "Stopped-flow studies of the refolding of iodoacetamide-blocked bovine serum albumin from the acid unfolded {"}F{"} state have been performed. If the protein is incubated with low concentrations of perchlorate anion then the refolding kinetics follow a simple first-order process. The dependence on pH of both the amplitude of the observed transients and the measured rate constants indicates that the N ⇌ F transition is highly cooperative. The results are consistent with the postulated multidomain structure of albumin which has been developed as a result of both sequence work and a variety of physical studies.",

author = "Taylor, {Ronald P.} and Vincent Chau and Zenkowich, {Mathew J.} and Leake, {Luther H.}",

note = "Funding Information: Suppart of this research by the National Science: Foundation (Grant No. PCM 7522703) is gratefully atknowledged. Preliminary stud& des&ked hwein have been supported by a Grant from the Virginia &st ks;ociation. RET is a &search Career Devefup-ment Awardee of the National fnstitutes of Health, No. ALOQ06203. Rw& far use-fuI discussions. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",

year = "1978",

month = jan,

doi = "10.1016/0301-4622(78)85006-6",

language = "English (US)",

volume = "7",

pages = "293--299",

journal = "Biophysical Chemistry",

issn = "0301-4622",

publisher = "Elsevier B.V.",

number = "4",

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TY - JOUR

T1 - Stopped-flow studies of the N ⇌ F transition in serum albumin

AU - Taylor, Ronald P.

AU - Chau, Vincent

AU - Zenkowich, Mathew J.

AU - Leake, Luther H.

N1 - Funding Information: Suppart of this research by the National Science: Foundation (Grant No. PCM 7522703) is gratefully atknowledged. Preliminary stud& des&ked hwein have been supported by a Grant from the Virginia &st ks;ociation. RET is a &search Career Devefup-ment Awardee of the National fnstitutes of Health, No. ALOQ06203. Rw& far use-fuI discussions. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.

PY - 1978/1

Y1 - 1978/1

N2 - Stopped-flow studies of the refolding of iodoacetamide-blocked bovine serum albumin from the acid unfolded "F" state have been performed. If the protein is incubated with low concentrations of perchlorate anion then the refolding kinetics follow a simple first-order process. The dependence on pH of both the amplitude of the observed transients and the measured rate constants indicates that the N ⇌ F transition is highly cooperative. The results are consistent with the postulated multidomain structure of albumin which has been developed as a result of both sequence work and a variety of physical studies.

AB - Stopped-flow studies of the refolding of iodoacetamide-blocked bovine serum albumin from the acid unfolded "F" state have been performed. If the protein is incubated with low concentrations of perchlorate anion then the refolding kinetics follow a simple first-order process. The dependence on pH of both the amplitude of the observed transients and the measured rate constants indicates that the N ⇌ F transition is highly cooperative. The results are consistent with the postulated multidomain structure of albumin which has been developed as a result of both sequence work and a variety of physical studies.

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DO - 10.1016/0301-4622(78)85006-6

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JO - Biophysical Chemistry

JF - Biophysical Chemistry

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ER -

Stopped-flow studies of the N ⇌ F transition in serum albumin

Abstract

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