A 96-kDa glycyrrhizin-binding protein (gp96) from soybeans acts as a substrate for casein kinase II, and is highly related to lipoxygenase 3.

A 96-kDa glycyrrhizin-binding protein (gp96) from soybeans acts as a substrate for casein kinase II, and is highly related to lipoxygenase 3. Research Abstract Details 

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A 96-kDa glycyrrhizin-binding protein (gp96) from soybeans acts as a substrate for casein kinase II, and is highly related to lipoxygenase 3. Abstract Text:

K Ohtsuki,S Nakamura,Y Shimoyama,D Shibata,H Munakata,Y Yoshiki,K Okubo,

A 96-kDa glycyrrhizin (GL)-binding protein (gp96) was purified to apparent homogeneity from an aqueous extract of soybeans by means of successive DEAE-cellulose column chromatography, gel filtration on Superdex 200pg, GL-affinity column chromatography, and ion-exchange chromatography on a Mono S column (HPLC). The protein was identified as a GL-binding protein since it specifically binds to [3H]GA. Moreover, it is a lipoxygenase (an enzyme that catalyzes the oxygenation of unsaturated fatty acids) since (i) it displays lipoxygenase (LOX) activity at pH 6.5; (ii) it is recognized on Western blot analysis by antibodies against LOX-1 and LOX-2; and (iii) the sequence of the N-terminal 21 amino acid residues (SNDVYLPRDEAFGHLKSSDFL) of a 42-kDa fragment (p42) proteolytically generated from gp96 is identical to a sequence of soybean LOX-3. In addition, GL, glycyrrhetinic acid (GA) and soyasaponin beta g slightly inhibited LOX activity of the purified gp96 fraction, whereas oGA (a GA derivative) greatly inhibited its activity. Furthermore, CK-II catalyzed phosphorylation of gp96 was stimulated significantly by GL at doses between 1 and 10 microM, but this phosphorylation was inhibited completely by 50 microM GL. All these results taken together suggest that (i) gp96 purified from soybeans as a GL-binding protein belongs to the LOX family; and (ii) triterpenoid saponins, including GL, are involved in the regulation of the activities of CK-II and LOXs in plants, such as soybeans and roots of liquorice, which contain large quantities of saponins.

A 96-kDa glycyrrhizin-binding protein (gp96) from soybeans acts as a substrate for casein kinase II, and is highly related to lipoxygenase 3. Publishing Authors By Initials

K Ohtsuki,S Nakamura,Y Shimoyama,D Shibata,H Munakata,Y Yoshiki,K Okubo,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

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A 96-kDa glycyrrhizin-binding protein (gp96) from soybeans acts as a substrate for casein kinase II, and is highly related to lipoxygenase 3. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 118

Page Numbers: 1145-50

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Dec

YEAR: 1995

A 96-kDa glycyrrhizin-binding protein (gp96) from soybeans acts as a substrate for casein kinase II, and is highly related to lipoxygenase 3. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

A 96-kDa glycyrrhizin-binding protein (gp96) from soybeans acts as a substrate for casein kinase II, and is highly related to lipoxygenase 3. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: metabolism

Chemical & Substance for Abstract: A 96-kDa glycyrrhizin-binding protein (gp96) from soybeans acts as a substrate for casein kinase II, and is highly related to lipoxygenase 3. Information

Substance Name: Protein-Serine-Threonine Kinases

Registry Number: EC 2.7.11.1

Grant and Affiliation Information for A 96-kDa glycyrrhizin-binding protein (gp96) from soybeans acts as a substrate for casein kinase II, and is highly related to lipoxygenase 3.

AFFILIATION: Laboratory of Genetical Biochemistry, Kitasato University School of Allied Health Sciences.

Country: JAPAN

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MEDLINETA: J Biochem

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