The Trypsin and Chymotrypsin Inhibitors from Avian Egg Whites

Rhodes, Marvin B.; Bennett, N. B.; Feeney, Robert E.

doi:10.1016/s0021-9258(19)76863-x

Cited by 171 publications

(28 citation statements)

References 22 publications

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“…Fractions 1 and 2 showed the greatest amount of antitryptic activity. These results appear similar to those of Rhodes et al (1960), who obtained three ovomucoid fractions with antitryptic activity for egg white fractionated on carboxymethylcellulose. Fractions 3 and 4 were devoid of antitryptic activity and the carbohydrate in these fractions was in the reducing form, indicating that it may be originating from free glucose or some degradation of the carbohydraterich moieties in the albumen.…”

Section: Resultssupporting

confidence: 90%

Characterization of the exudate from cooked shell eggs

Nath¹,

Vadehra²,

Baker³

1972

J. Agric. Food Chem.

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Boiled and peeled eggs stored in Cryovac bags at 5°C produced a greenish-yellow fluorescent exudate.The amount of exudate increased from 1.26% at 1 day to 2.7% at 7 days, with no further increase on storage. The freeze-dried exudate contained 61 % protein, 21.25% carbohydrate, and 8.9% minerals.Chromatography of the exudate on Sephadex G-50 produced five fractions. The first two fractions, based on biological activity and chemical analysis, appeared to be ovomucoid-like. Fractions 3 and 4 contained large amounts of carbohydrate but their exact nature could not be established. Fraction 5 was fluorescent and appeared to be a component of the flavoprotein moiety in albumen.

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Section: Resultssupporting

confidence: 90%

Characterization of the exudate from cooked shell eggs

Nath¹,

Vadehra²,

Baker³

1972

J. Agric. Food Chem.

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“…Probably the most remarkable work on avian ovomucoids is the paper of Rhodes et al (1960), who isolated ovomucoids from egg whites of several species of birds and studied their inhibitory properties. They found that ovomucoids from closely related species often have strikingly different inhibitory specificities.…”

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confidence: 99%

“…We had used chicken ovomucoid along with soybean trypsin inhibitor (Kunitz) in our early studies of protein inhibitors of serine proteinase (Finkenstadt & Laskowski, 1965;Ozawa & Laskowski, 1966), but we knew little about its chemical or three-dimensional structure. The other motive was the work of Rhodes et al (1960), which suggested that ovomucoids were an excellent system for the study of the relationship between sequence and reactivity of proteinase inhibitors.…”

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confidence: 99%

Chicken ovomucoid: determination of its amino acid sequence, determination of the trypsin reactive site, and preparation of all three of its domains

Kato¹,

Schrode²,

Kohr³

et al. 1987

Biochemistry

200

123

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The complete amino acid sequence of chicken ovomucoid (OMCHI) is presented. OMCHI consists of three tandem domains, each homologous to pancreatic secretory trypsin inhibitor (Kazal) and each with an actual or putative reactive site for inhibition of serine proteinases. The major reactive site for bovine beta-trypsin is the Arg89-Ala peptide bond in the second domain. The equilibrium constant for hydrolysis of this peptide bond, K0hyd, is 1.85. The first and third domains of OMCHI are relatively ineffective inhibitors of several serine proteinases against which they were tested. OMCHI is a mixture of two forms: the major form with all of the amino acid residues and a minor form with Val134-Ser135 deleted. This polymorphism is present in all chicken eggs and is the result of ambiguous excision at the 5' end of the F intron. Procedures are given for preparation of modified chicken ovomucoid, OMCHI (in which the Arg89-Ala bond is hydrolyzed), of the first domain, OMCHI1 (residues 1-68), of the second domain, OMCHI2 (residues 65-130), and of the third domain, OMCHI3 (residues 131-186). In the case of the third domain, both the Asn175 glycosylated form, OMCHI3(+), and the carbohydrate-free form, OMCHI3(-), were obtained. These isolated native domains are useful in many studies of ovomucoid behavior.

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“…After the reaction was performed at 30 °C for 10 min, it was stopped by adding 4% trichloroacetic acid, and absorbancy of the filtrate at 280 nm was measured. TI and CTI were also determined by the spectrophotometric method of Rhodes et al (1960) using toluenesulfonyl-L-arginine methyl ester (TAME) and benzoyl-L-tyrosine ethyl ester (BTE) as the substrate, respectively.…”

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2S globulins of soybean seeds. 1. Isolation and characterization of protein components

Koshiyama¹,

Kikuchi²,

Harada³

et al. 1981

J. Agric. Food Chem.

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The 2S globulins of soybean seeds have been recognized to be storage proteins without biological activities for a long time. There are two immunologically different antigens and six bands by disc electrophoresis. Among them, three major bands occupying ~80% of the globulins were isolated by DEAE-Sephadex chromatography. In opposition of the recognition so far, all peaks from the chromatography had some inhibitory activities against trypsin and/or -chymotrypsin. Two of three major fractions designated as a3 and a4 protein were immunologically identical with each other but entirely different from the remaining one, designated as a2 protein. From the distribution of the three major fractions in the 2S globulins, Japanese varieties belonged almost entirely to the a3 or a4 type but American varieties belonged almost entirely to the a3 type. a3 protein was identical with the Kunitz trypsin inhibitor, and a4 was estimated to be a size isomer of a3 protein.Ultracentrifugal investigations have classically shown that soybean storage proteins (soybean globulins) consist of four components with sedimentation constants equal to about 2, 7,11, and 15 S. Soybean globulins have been recognized to be storage proteins because of no biological activities and the location in cotyledonous subcellular particles called "protein bodies". Among them, the major components in the 7S and US fractions have been well investigated in many laboratories. The 2S fraction is not composed of only one protein component, but some protein components have been suggested to exist in the fraction (Vaintraub, 1965; Wolf and Sly, 1965). Moreover, two ultracentrifugally pure proteins, 2.3S and 2.8S globulins, by Vaintraub and Shutov (1969) and an antigenic protein, -conglycinin, by Catsimpoolas and Ekenstam (1969) have been isolated from the 2S fraction of soybean globulin.-Conglycinin has been reported to have no activities of protease inhibitions. However, the 2S fraction is not always still well understood.Recently, we have found that there is a strong allergenicity for food hypersensitivity of soybean proteins mediated by immunoglobulin E (IgE) antibody using a radioallergosolvent test (RAST) in the 2S fraction (unpublished results). Accordingly, it is very important to clarify the protein components in the 2S fraction of soybean globulins.This paper reports the fractionation of the 2S fraction and the characterization of the fractionated components. EXPERIMENTAL SECTION Materials. Soybeans of Japanese varieties were obtained from Chushin Agricultural Experimental Station,

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The Trypsin and Chymotrypsin Inhibitors from Avian Egg Whites

Cited by 171 publications

References 22 publications

Characterization of the exudate from cooked shell eggs

Characterization of the exudate from cooked shell eggs

Chicken ovomucoid: determination of its amino acid sequence, determination of the trypsin reactive site, and preparation of all three of its domains

2S globulins of soybean seeds. 1. Isolation and characterization of protein components

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