Properties and Food Uses of Duck Eggs ,

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

doi:10.3382/ps.0391473

Cited by 23 publications

(20 citation statements)

References 6 publications

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“…the routine assay. Under these conditions the enzymes were still inhibited, since no increax in enzymatic activity over the slight activities (5-15Oj,) which these enzyme-inhibitor complexes normally show (Gorini and Audrain, 1953;Rhodes et al, 1960) was detected. In control experiments both trypsin and chymotrypsin were fully active in the presence of 3 M urea, indicating that urea, in the concentrations used, does not dissociate the enzyme-inhibitor complexes.…”

Section: Stability To Trichloroacetic Acid-acetone Treatment -mentioning

confidence: 90%

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Chemical Modification of Avian Ovomucoids^*

Stevens¹,

Feeney²

1963

Biochemistry

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Comparative physical and chemical studies were performed on three avian qvomucoids: chicken ovomucoid (a trypsin inhibitor), turkey ovomucoid (a trypsin and chymotryps ininhibitor), and pheasant ovomucoid (a chymotrypsin inhibitor). The amino acid composition and the carbohydrate contents have been determined. All three ovomucoids are stable to heating a t 80 ' at pH < 9, but heating to 100 O at p H 6 or to 80 O a t pH 9 results in a rapid loss of inhibitory activity for all three ovomucoids. They are also resistant to treatment with trichloroacetic acidacetone and 9 M urea a t 80 ' . Their complexes with the respective enzymes are not affected by 3 M urea. Acetylation with acetic anhydride or carbamylation with KNCO destroy the trypsin inhibitory activity of turkey ovomucoid, while they leave its chymotrypsin inhibitory activity and the inhibitory activities of the other ovomucoids unaffected. It appeared that the structural requirements of turkey and chicken ovomucoids for inhibiting trypsin are different and that the inhibitory sites of turkey ovomucoid for trypsin and for chymotrypsin are independent.Extensive iodination has no effect on any of the inhibitory activities.

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Section: Stability To Trichloroacetic Acid-acetone Treatment -mentioning

confidence: 90%

“…Inhibitor Assays.-Unless otherwise indicated, assays were made by the spectrophotometric method described previously (Feeney et al, 1963; Rhodes et al, 1960) using synthetic substrates and an acid-base indicator (in a Beckman Model DB spectrophotometer with…”

Section: Methodsmentioning

confidence: 99%

Chemical Modification of Avian Ovomucoids^*

Stevens¹,

Feeney²

1963

Biochemistry

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“…Thus, the classical observation by Kunitz [15] that STI not only inhibits trypsin but also weakly inhibits chymotrypsin, was taken to suggest that STI contains another reactive site that recognizes chymotrypsin. This was not unusual since at that time many multi-headed inhibitors such as ovomucoid and BowmannBirk inhibitor [16,17] were already known which inhibited trypsin and chymotrypsin at separate reactive sites.…”

Section: Different Serine Proteinases Are Inhibited By the Same Reactmentioning

confidence: 93%

“…The focus of his research started shifting from STI to ovomucoids in early 1970s. The presence of high concentrations of an inhibitory protein, ovomucoid, in avian eggs was already known [16]. It had also been shown that some ovomucoids were 'triple headed', meaning that one ovomucoid molecule could inhibit up to three proteinase molecules.…”

Section: Ovomucoid Third Domainsmentioning

confidence: 96%

From the Discovery of the Reactive Site of Inhibitors to Their Sequence to Reactivity Algorithm

Qasim

2005

PPL

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Michael Laskowski Jr. (1930-2004) was a pioneer in the field of Standard mechanism serine proteinase inhibitors. He made numerous important contributions in the field. This article highlights some of his most important contributions such as the discovery of the reactive site in serine proteinase inhibitors, the proposal of the Standard mechanism of inhibition, and the sequence to reactivity algorithm for the Kazal family of inhibitors.

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“…Hydrolyses of Glt-Phe-ANp and Suc-Phe-ANp were carried out by the method of Erlanger' 19 Mn almost the same way. Hydrolyses of Bz-TyrOEt, Z-Tyr-ONp, and Ac-ONp were also carried out by measuring the changes in ultraviolet absorbance, according to Rhodes et alJ 20] , Lorand et alJ 21 Preparation of the a^globulin fraction of bovine serum by paper electrophoresis^1 6 1 On a sheet of filter paper (Toyo No. 51) of 25 χ 40 cm area, 2 lines were drawn longitudinally, 3 cm from each side, and 21 lines transversely at 1-cm intervals.…”

Section: Activity Measurementsmentioning

confidence: 99%

The Effect of α₂-Macroglobulin from Bovine Serum on Bovine α-Chymotrypsin

Nakamura¹,

Ogata²,

Takeo³

et al. 1975

Hoppe-Seyler´s Zeitschrift für physiologische Chemie

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Bovine a 2 -globulin contains a protein which increases the activity of bovine a-chymotrypsin against synthetic substrates. The active protein fraction migrates slowly on polyacrylamide gel electrophoresis, so it was named slow a 2 -globulin (Sa 2 ). The fraction was isolated from bovine serum and purified. Its sedimentation constant s 2 o was 18.5 S. It was thus identified with the a 2 -macroglobulin (a 2 M). By kinetic studies, the dissociation constant of the a-chymotrypsin-a 2 M complex was calculated to be of the order of 10~7 //mol. The purified a 2 M was shown to bind -chymotrypsin at a definite rate. If the binding ratio was assumed to be 1:2, the molecular weight was calculated to be about 8xl0 5 . Einfluß von & 2 -Makroglobulin des Rinderserums auf a-Chymotrypsin des RindesZusammenfassung: Das a 2 -Globulin des Rinderserums enthält ein Eiweiß, welches die Aktivität von -Chymotrypsin für die synthetischen Substrate beträchtlich steigert. Die aktive Eiweiß-fraktion wandert langsam in der Polyakrylamidgel-Elektrophorese und wird Slow-a 2 -Globulin genannt. Die betreffende Eiweißfraktion wurde aus dem Rinderserum isoliert und gereinigt. Seine Sedimentationskonstante s 20 war 18.5 S. Daher wurde es mit dem a 2 -Makroglobulin (a 2 M) identifiziert. Die Dissoziationskonstante des Komplexes des -Chymotrypsins mit dem a 2 M wurde durch kinetische Untersuchungen ermittelt und war in der Größenordnung von 10~7 //mol. Es wurde bestätigt, daß das gereinigte a 2 M mit dem -Chymotrypsin in einem bestimmten Verhält-nis gebunden wurde. Nimmt man ein molekulares Bindungsverhältnis von l :2 an, so läßt sich sein Molekulargewicht zu ungefähr 8 10 s berechnen.

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Properties and Food Uses of Duck Eggs ,

Cited by 23 publications

References 6 publications

Chemical Modification of Avian Ovomucoids^*

Chemical Modification of Avian Ovomucoids^*

From the Discovery of the Reactive Site of Inhibitors to Their Sequence to Reactivity Algorithm

The Effect of α₂-Macroglobulin from Bovine Serum on Bovine α-Chymotrypsin

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Properties and Food Uses of Duck Eggs ,

Cited by 23 publications

References 6 publications

Chemical Modification of Avian Ovomucoids*

Chemical Modification of Avian Ovomucoids*

From the Discovery of the Reactive Site of Inhibitors to Their Sequence to Reactivity Algorithm

The Effect of α2-Macroglobulin from Bovine Serum on Bovine α-Chymotrypsin

Contact Info

Product

Resources

About

Chemical Modification of Avian Ovomucoids^*

Chemical Modification of Avian Ovomucoids^*

The Effect of α₂-Macroglobulin from Bovine Serum on Bovine α-Chymotrypsin