Degree of dissociation of apohemoglobin studied by nanosecond fluorescence-polarization technique

Kazuhiko Kinosita; Shigeki Mitaku; Akira Ikegami

doi:10.1016/0005-2795(75)90210-X

Degree of dissociation of apohemoglobin studied by nanosecond fluorescence-polarization technique

Kazuhiko Kinosita^*, Shigeki Mitaku, Akira Ikegami

^*Corresponding author for this work

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

Abstract

A fluorescent dye 1-anilino-8-naphthalene sulfonate was complexed with human apohemoglobin and sperm whale apomyoglobin. Nanosecond fluorescencepolarization kinetics were measured for each of these complexes in KCl solutions to obtain their fluorescence lifetimes and rotational correlation times. The rotational correlation time of apohemoglobin-dye complex was found to be 21 ns, which was about twice that of apomyoglobin-dye complex, 11 ns. These values were constant over an ionic strength range from 0 to 1.7. Circular dichroism spectra (215-300 nm) and fluorescence lifetimes of the complexes were also found to be independent of the ionic strength, indicating that no gross conformational change occurs with the change in the salt concentration. These results suggest that apohemoglobin remains dimeric over the ionic-strength range examined.

Original language	English
Pages (from-to)	10-14
Number of pages	5
Journal	BBA - Protein Structure
Volume	393
Issue number	1
DOIs	https://doi.org/10.1016/0005-2795(75)90210-X
Publication status	Published - 1975 May 30
Externally published	Yes

ASJC Scopus subject areas

Medicine(all)

Access to Document

10.1016/0005-2795(75)90210-X

Cite this

@article{9f6c10b1d68241f39e219fbcae91f10f,

title = "Degree of dissociation of apohemoglobin studied by nanosecond fluorescence-polarization technique",

abstract = "A fluorescent dye 1-anilino-8-naphthalene sulfonate was complexed with human apohemoglobin and sperm whale apomyoglobin. Nanosecond fluorescencepolarization kinetics were measured for each of these complexes in KCl solutions to obtain their fluorescence lifetimes and rotational correlation times. The rotational correlation time of apohemoglobin-dye complex was found to be 21 ns, which was about twice that of apomyoglobin-dye complex, 11 ns. These values were constant over an ionic strength range from 0 to 1.7. Circular dichroism spectra (215-300 nm) and fluorescence lifetimes of the complexes were also found to be independent of the ionic strength, indicating that no gross conformational change occurs with the change in the salt concentration. These results suggest that apohemoglobin remains dimeric over the ionic-strength range examined.",

author = "Kazuhiko Kinosita and Shigeki Mitaku and Akira Ikegami",

year = "1975",

month = may,

day = "30",

doi = "10.1016/0005-2795(75)90210-X",

language = "English",

volume = "393",

pages = "10--14",

journal = "BBA - Protein Structure",

issn = "1570-9639",

publisher = "Elsevier",

number = "1",

}

TY - JOUR

T1 - Degree of dissociation of apohemoglobin studied by nanosecond fluorescence-polarization technique

AU - Kinosita, Kazuhiko

AU - Mitaku, Shigeki

AU - Ikegami, Akira

PY - 1975/5/30

Y1 - 1975/5/30

N2 - A fluorescent dye 1-anilino-8-naphthalene sulfonate was complexed with human apohemoglobin and sperm whale apomyoglobin. Nanosecond fluorescencepolarization kinetics were measured for each of these complexes in KCl solutions to obtain their fluorescence lifetimes and rotational correlation times. The rotational correlation time of apohemoglobin-dye complex was found to be 21 ns, which was about twice that of apomyoglobin-dye complex, 11 ns. These values were constant over an ionic strength range from 0 to 1.7. Circular dichroism spectra (215-300 nm) and fluorescence lifetimes of the complexes were also found to be independent of the ionic strength, indicating that no gross conformational change occurs with the change in the salt concentration. These results suggest that apohemoglobin remains dimeric over the ionic-strength range examined.

AB - A fluorescent dye 1-anilino-8-naphthalene sulfonate was complexed with human apohemoglobin and sperm whale apomyoglobin. Nanosecond fluorescencepolarization kinetics were measured for each of these complexes in KCl solutions to obtain their fluorescence lifetimes and rotational correlation times. The rotational correlation time of apohemoglobin-dye complex was found to be 21 ns, which was about twice that of apomyoglobin-dye complex, 11 ns. These values were constant over an ionic strength range from 0 to 1.7. Circular dichroism spectra (215-300 nm) and fluorescence lifetimes of the complexes were also found to be independent of the ionic strength, indicating that no gross conformational change occurs with the change in the salt concentration. These results suggest that apohemoglobin remains dimeric over the ionic-strength range examined.

UR - http://www.scopus.com/inward/record.url?scp=0016822935&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0016822935&partnerID=8YFLogxK

U2 - 10.1016/0005-2795(75)90210-X

DO - 10.1016/0005-2795(75)90210-X

M3 - Article

C2 - 1138915

AN - SCOPUS:0016822935

SN - 1570-9639

VL - 393

SP - 10

EP - 14

JO - BBA - Protein Structure

JF - BBA - Protein Structure

IS - 1

ER -

Degree of dissociation of apohemoglobin studied by nanosecond fluorescence-polarization technique

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this