Studies on the structures of haptoglobin 1-1 and hemoglobin in the haptoglobin-hemoglobin complex

Marcel Waks; Peter C. Kahn; Sherman Beychok

doi:https://doi.org/10.1016/0006-291X(71)90150-1

Studies on the structures of haptoglobin 1-1 and hemoglobin in the haptoglobin-hemoglobin complex

Marcel Waks, Peter C. Kahn, Sherman Beychok

SEBS - Biochem & Microbiology

Rutgers, The State University

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

8 Scopus citations

Abstract

The near and far ultraviolet (UV) circular dichroism (CD) spectra of human haptoglobin 1-1 (Hp 1-1) and of one of its complexes with horse ferrihemoglobin are presented. Comparison of the far UV spectrum of the complex with the appropriate weighted sum of its components gives a calculated spectrum that is slightly more negative than the experimental at every wavelength. The small deviation from additivity indicates that if any changes in secondary structure occur on complex formation, they are very small. The basic chain folding of the hemoglobin is preserved, at least with regard to helix content. Changes in side-chain and heme optical activity cause similar deviations from additivity in the near UV and these may be responsible for the observed far UV deviations.

Original language	English (US)
Pages (from-to)	1232-1239
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	45
Issue number	5
DOIs	https://doi.org/10.1016/0006-291X(71)90150-1
State	Published - Dec 3 1971

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Studies on the structures of haptoglobin 1-1 and hemoglobin in the haptoglobin-hemoglobin complex",

abstract = "The near and far ultraviolet (UV) circular dichroism (CD) spectra of human haptoglobin 1-1 (Hp 1-1) and of one of its complexes with horse ferrihemoglobin are presented. Comparison of the far UV spectrum of the complex with the appropriate weighted sum of its components gives a calculated spectrum that is slightly more negative than the experimental at every wavelength. The small deviation from additivity indicates that if any changes in secondary structure occur on complex formation, they are very small. The basic chain folding of the hemoglobin is preserved, at least with regard to helix content. Changes in side-chain and heme optical activity cause similar deviations from additivity in the near UV and these may be responsible for the observed far UV deviations.",

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T1 - Studies on the structures of haptoglobin 1-1 and hemoglobin in the haptoglobin-hemoglobin complex

AU - Waks, Marcel

AU - Kahn, Peter C.

AU - Beychok, Sherman

PY - 1971/12/3

Y1 - 1971/12/3

N2 - The near and far ultraviolet (UV) circular dichroism (CD) spectra of human haptoglobin 1-1 (Hp 1-1) and of one of its complexes with horse ferrihemoglobin are presented. Comparison of the far UV spectrum of the complex with the appropriate weighted sum of its components gives a calculated spectrum that is slightly more negative than the experimental at every wavelength. The small deviation from additivity indicates that if any changes in secondary structure occur on complex formation, they are very small. The basic chain folding of the hemoglobin is preserved, at least with regard to helix content. Changes in side-chain and heme optical activity cause similar deviations from additivity in the near UV and these may be responsible for the observed far UV deviations.

AB - The near and far ultraviolet (UV) circular dichroism (CD) spectra of human haptoglobin 1-1 (Hp 1-1) and of one of its complexes with horse ferrihemoglobin are presented. Comparison of the far UV spectrum of the complex with the appropriate weighted sum of its components gives a calculated spectrum that is slightly more negative than the experimental at every wavelength. The small deviation from additivity indicates that if any changes in secondary structure occur on complex formation, they are very small. The basic chain folding of the hemoglobin is preserved, at least with regard to helix content. Changes in side-chain and heme optical activity cause similar deviations from additivity in the near UV and these may be responsible for the observed far UV deviations.

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JO - Biochemical and Biophysical Research Communications

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Studies on the structures of haptoglobin 1-1 and hemoglobin in the haptoglobin-hemoglobin complex

Abstract

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