Lysine-Rich Proteins in High-Lysine Hordeum Vulgare Grain

J. Ingversen; B. Køie

doi:10.1016/0031-9422(73)85024-1

Lysine-Rich Proteins in High-Lysine Hordeum Vulgare Grain

J. Ingversen, B. Køie

Research output: Contribution to journal › Journal article › Research › peer-review

Abstract

The salt-soluble proteins in barley grain selected for high-lysine content (Hiproly, CI 7115 and the mutants 29 and 86) and of a control (Carlsberg II) with normal lysine content, contain identical major proteins as determined by MW and electrophoretic mobility. The concentration of a protein group with a high lysine content varies significantly among the barleys examined. One protein, present in large amounts in Hiproly, is assumed to be partially responsible for the high-lysine character of Hiproly, CI 7115 and the mutants 29 and 86.

Original language	English
Journal	Phytochemistry
Volume	12
Issue number	5
Pages (from-to)	1107-1111
ISSN	0031-9422
DOIs	https://doi.org/10.1016/0031-9422(73)85024-1
Publication status	Published - 1973

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title = "Lysine-Rich Proteins in High-Lysine Hordeum Vulgare Grain",

abstract = "The salt-soluble proteins in barley grain selected for high-lysine content (Hiproly, CI 7115 and the mutants 29 and 86) and of a control (Carlsberg II) with normal lysine content, contain identical major proteins as determined by MW and electrophoretic mobility. The concentration of a protein group with a high lysine content varies significantly among the barleys examined. One protein, present in large amounts in Hiproly, is assumed to be partially responsible for the high-lysine character of Hiproly, CI 7115 and the mutants 29 and 86.",

author = "J. Ingversen and B. K{\o}ie",

year = "1973",

doi = "10.1016/0031-9422(73)85024-1",

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journal = "Phytochemistry",

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T1 - Lysine-Rich Proteins in High-Lysine Hordeum Vulgare Grain

AU - Ingversen, J.

AU - Køie, B.

PY - 1973

Y1 - 1973

N2 - The salt-soluble proteins in barley grain selected for high-lysine content (Hiproly, CI 7115 and the mutants 29 and 86) and of a control (Carlsberg II) with normal lysine content, contain identical major proteins as determined by MW and electrophoretic mobility. The concentration of a protein group with a high lysine content varies significantly among the barleys examined. One protein, present in large amounts in Hiproly, is assumed to be partially responsible for the high-lysine character of Hiproly, CI 7115 and the mutants 29 and 86.

AB - The salt-soluble proteins in barley grain selected for high-lysine content (Hiproly, CI 7115 and the mutants 29 and 86) and of a control (Carlsberg II) with normal lysine content, contain identical major proteins as determined by MW and electrophoretic mobility. The concentration of a protein group with a high lysine content varies significantly among the barleys examined. One protein, present in large amounts in Hiproly, is assumed to be partially responsible for the high-lysine character of Hiproly, CI 7115 and the mutants 29 and 86.

U2 - 10.1016/0031-9422(73)85024-1

DO - 10.1016/0031-9422(73)85024-1

M3 - Journal article

SN - 0031-9422

VL - 12

SP - 1107

EP - 1111

JO - Phytochemistry

JF - Phytochemistry

IS - 5

ER -

Lysine-Rich Proteins in High-Lysine Hordeum Vulgare Grain

Abstract

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