An isoleucine-valine substitution in the β chain of rabbit hemoglobin

James Bricker; Michael D. Garrick

doi:10.1016/0005-2795(74)90208-6

An isoleucine-valine substitution in the β chain of rabbit hemoglobin

James Bricker
, Michael D. Garrick

Biochemistry

SUNY Buffalo

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

17 Scopus citations

Abstract

We have characterized a variant hemoglobin in which the β chain lacks isoleucine at position 112. Isolated β chains were digested with formic acid, which cleaved the aspartyl-prolyl linkage (residues 99-100). The peptide fraction containing β112 was purified and then sequenced in an automatic sequencer. Valine replaced isoleucine in the variant chain.

Original language	English
Pages (from-to)	437-441
Number of pages	5
Journal	BBA - Protein Structure
Volume	351
Issue number	2
DOIs	https://doi.org/10.1016/0005-2795(74)90208-6
State	Published - Jun 7 1974

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title = "An isoleucine-valine substitution in the β chain of rabbit hemoglobin",

abstract = "We have characterized a variant hemoglobin in which the β chain lacks isoleucine at position 112. Isolated β chains were digested with formic acid, which cleaved the aspartyl-prolyl linkage (residues 99-100). The peptide fraction containing β112 was purified and then sequenced in an automatic sequencer. Valine replaced isoleucine in the variant chain.",

author = "James Bricker and Garrick, \{Michael D.\}",

year = "1974",

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T1 - An isoleucine-valine substitution in the β chain of rabbit hemoglobin

AU - Bricker, James

AU - Garrick, Michael D.

PY - 1974/6/7

Y1 - 1974/6/7

N2 - We have characterized a variant hemoglobin in which the β chain lacks isoleucine at position 112. Isolated β chains were digested with formic acid, which cleaved the aspartyl-prolyl linkage (residues 99-100). The peptide fraction containing β112 was purified and then sequenced in an automatic sequencer. Valine replaced isoleucine in the variant chain.

AB - We have characterized a variant hemoglobin in which the β chain lacks isoleucine at position 112. Isolated β chains were digested with formic acid, which cleaved the aspartyl-prolyl linkage (residues 99-100). The peptide fraction containing β112 was purified and then sequenced in an automatic sequencer. Valine replaced isoleucine in the variant chain.

UR - https://www.scopus.com/pages/publications/0016160162

U2 - 10.1016/0005-2795(74)90208-6

DO - 10.1016/0005-2795(74)90208-6

M3 - Article

C2 - 4407315

AN - SCOPUS:0016160162

SN - 0005-2795

VL - 351

SP - 437

EP - 441

JO - BBA - Protein Structure

JF - BBA - Protein Structure

IS - 2

ER -

An isoleucine-valine substitution in the β chain of rabbit hemoglobin

Abstract

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