The comparative enzymology of lactic dehydrogenases. II. Properties of the crystalline HM3 hybrid from chicken muscle and of H2M2 hybrid and H4 enzyme from chicken liver

Thomas P Fondy, Amadeo Pesce, Irwin Freedberg, Francis Stolzenbach, Nathan O. Kaplan

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

The hybrid lactic dehydrogenases H2M2 from chicken liver and HM3 from chicken leg muscle have been isolated and crystallized. The pure H4 form of the enzyme has been isolated and crystallized from chicken liver and compared to the H4 obtained from heart. Fingerprint patterns of tryptic digests of the hybrids have been compared to patterns obtained from a 1:1 mixture of the H4 and M4 and have shown the hybrids to be a combination of the pure forms. Amino acid analyses, particularly of histidine, place the hybrids at points intermediate between the pure types. The H4 from chicken liver did not vary significantly in amino acid content or molecular weight from the H4 obtained from chicken heart. Molecular weights of the hybrids were in the same range as those of the pure types. Heat and time stability studies of the chicken hybrids and of beef hybrids isolated from starch grain have established the intermediate nature of the hybrids. Immunological properties, analog ratios, and oxalate inhibition also demonstrate that the hybrids are combinations of the H4 and M4 forms of the enzyme.

Original languageEnglish (US)
Pages (from-to)522-530
Number of pages9
JournalBiochemistry
Volume3
Issue number4
StatePublished - 1964
Externally publishedYes

Fingerprint

Liver
Muscle
Chickens
Oxidoreductases
Milk
Crystalline materials
Muscles
Enzymes
Molecular weight
Amino Acids
Beef
Oxalates
Histidine
Starch
Molecular Weight
Dermatoglyphics
Leg
Hot Temperature

ASJC Scopus subject areas

  • Biochemistry

Cite this

The comparative enzymology of lactic dehydrogenases. II. Properties of the crystalline HM3 hybrid from chicken muscle and of H2M2 hybrid and H4 enzyme from chicken liver. / Fondy, Thomas P; Pesce, Amadeo; Freedberg, Irwin; Stolzenbach, Francis; Kaplan, Nathan O.

In: Biochemistry, Vol. 3, No. 4, 1964, p. 522-530.

Research output: Contribution to journalArticle

@article{73c284e39db24582b5d35d092fed3b97,
title = "The comparative enzymology of lactic dehydrogenases. II. Properties of the crystalline HM3 hybrid from chicken muscle and of H2M2 hybrid and H4 enzyme from chicken liver",
abstract = "The hybrid lactic dehydrogenases H2M2 from chicken liver and HM3 from chicken leg muscle have been isolated and crystallized. The pure H4 form of the enzyme has been isolated and crystallized from chicken liver and compared to the H4 obtained from heart. Fingerprint patterns of tryptic digests of the hybrids have been compared to patterns obtained from a 1:1 mixture of the H4 and M4 and have shown the hybrids to be a combination of the pure forms. Amino acid analyses, particularly of histidine, place the hybrids at points intermediate between the pure types. The H4 from chicken liver did not vary significantly in amino acid content or molecular weight from the H4 obtained from chicken heart. Molecular weights of the hybrids were in the same range as those of the pure types. Heat and time stability studies of the chicken hybrids and of beef hybrids isolated from starch grain have established the intermediate nature of the hybrids. Immunological properties, analog ratios, and oxalate inhibition also demonstrate that the hybrids are combinations of the H4 and M4 forms of the enzyme.",
author = "Fondy, {Thomas P} and Amadeo Pesce and Irwin Freedberg and Francis Stolzenbach and Kaplan, {Nathan O.}",
year = "1964",
language = "English (US)",
volume = "3",
pages = "522--530",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "4",

}

TY - JOUR

T1 - The comparative enzymology of lactic dehydrogenases. II. Properties of the crystalline HM3 hybrid from chicken muscle and of H2M2 hybrid and H4 enzyme from chicken liver

AU - Fondy, Thomas P

AU - Pesce, Amadeo

AU - Freedberg, Irwin

AU - Stolzenbach, Francis

AU - Kaplan, Nathan O.

PY - 1964

Y1 - 1964

N2 - The hybrid lactic dehydrogenases H2M2 from chicken liver and HM3 from chicken leg muscle have been isolated and crystallized. The pure H4 form of the enzyme has been isolated and crystallized from chicken liver and compared to the H4 obtained from heart. Fingerprint patterns of tryptic digests of the hybrids have been compared to patterns obtained from a 1:1 mixture of the H4 and M4 and have shown the hybrids to be a combination of the pure forms. Amino acid analyses, particularly of histidine, place the hybrids at points intermediate between the pure types. The H4 from chicken liver did not vary significantly in amino acid content or molecular weight from the H4 obtained from chicken heart. Molecular weights of the hybrids were in the same range as those of the pure types. Heat and time stability studies of the chicken hybrids and of beef hybrids isolated from starch grain have established the intermediate nature of the hybrids. Immunological properties, analog ratios, and oxalate inhibition also demonstrate that the hybrids are combinations of the H4 and M4 forms of the enzyme.

AB - The hybrid lactic dehydrogenases H2M2 from chicken liver and HM3 from chicken leg muscle have been isolated and crystallized. The pure H4 form of the enzyme has been isolated and crystallized from chicken liver and compared to the H4 obtained from heart. Fingerprint patterns of tryptic digests of the hybrids have been compared to patterns obtained from a 1:1 mixture of the H4 and M4 and have shown the hybrids to be a combination of the pure forms. Amino acid analyses, particularly of histidine, place the hybrids at points intermediate between the pure types. The H4 from chicken liver did not vary significantly in amino acid content or molecular weight from the H4 obtained from chicken heart. Molecular weights of the hybrids were in the same range as those of the pure types. Heat and time stability studies of the chicken hybrids and of beef hybrids isolated from starch grain have established the intermediate nature of the hybrids. Immunological properties, analog ratios, and oxalate inhibition also demonstrate that the hybrids are combinations of the H4 and M4 forms of the enzyme.

UR - http://www.scopus.com/inward/record.url?scp=33747829700&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33747829700&partnerID=8YFLogxK

M3 - Article

C2 - 14188168

AN - SCOPUS:33747829700

VL - 3

SP - 522

EP - 530

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 4

ER -