Physical characterization of ovoinhibitor, a trypsin and chymotrypsin inhibitor from chicken egg white

Tomimatsu, Yoshio; Clary, John J.; Bartulovich, John J.

doi:10.1016/0003-9861(66)90073-7

Cited by 89 publications

(42 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…B08 was designated to ovoinhibitor precursor (Gallus gallus), while duck ovoinhibitor was not identified in duck. As a trypsin and chymotrypsin inhibitor, [37] ovoinhibitor has been found in the egg white of chicken, quail, and ostrich. [11] Its deficiency in duck egg white may suggest weaker inhibition of endogenous protease activity and shorter storage period than those of chicken and quail eggs.…”

Section: Resultsmentioning

confidence: 99%

Comparative proteomic analysis of chicken, duck, and quail egg yolks

Liu

Qiu

Гао

et al. 2018

International Journal of Food Properties

View full text Add to dashboard Cite

A comparative analysis of egg yolk proteome of three major poultry species, namely, chicken, duck, and quail, was carried out with two-dimensional (2D) gel electrophoresis patterns and matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry. Proteins identified from these three poultry species shared high degrees of sequence and structure homology, which might be related to the bird's adaptability under different environmental stresses. Few specific proteins were found in this study. Comparative 2D gel electrophoresis patterns of chicken, duck, and quail revealed that some protein-specific regions on gels could be used for authentic identification of poultry eggs. These findings could provide a fundamental understanding of different poultry egg protein profiles and showed us some new sights in egg yolk nutrients related to certain properties and functions.ARTICLE HISTORY

show abstract

Section: Resultsmentioning

confidence: 99%

Comparative proteomic analysis of chicken, duck, and quail egg yolks

Liu

Qiu

Гао

et al. 2018

International Journal of Food Properties

View full text Add to dashboard Cite

show abstract

“…All assays were carried out a t 23 "C, pH 8.0, in 0.2 M Tris-HC1 buffer, containing 0.02; CaC1,. A unit of tryptic or chymotryptic activity was defined as the absorbance change per minute per mg bovine enzyme.…”

Section: Activity Measurementsmentioning

confidence: 99%

Human Pancreatic Proteolytic Enzymes and Protein Inhibitors

Feinstein

Hofstein

Koifmann

et al. 1974

European Journal of Biochemistry

View full text Add to dashboard Cite

The purification of human proteolytic enzymes, i.e. two trypsins, two chymotrypsins and a t least one elastase from activated extracts of human pancreas has been accomplished by a combination of a,ffinity chromatography and conventional ion-exchange chromatography on XE-Xephadex. The enzymes thus obtained were homogeneous by several criteria : gel electrophoresis, equilibrium sedimentation and immunological assay. The molecular weight and amino-acid composition of each preparation was determined and compared with those of other mammalian enzymes. The two trypsins showed only partial immunological identity while the two chymotrypsins were identical immunologically. The data raises the question of the number of the zymogens present in the human pancreas.I n addition to the proteolytic enzymes, four protein inhibitors of proteolytic enzymes were also isolated from human pancreas. The procedure consisted of several steps that included gel filtration, affinity chromatography and isoelectric focusing. The two major components which accounted for most of the trypsin inhibitory activity were characterized and were apparently of the Kazal type. The more basic human pancreatic inhibitor had a p I of 8.7 and contained 48 amino acids with a molecular weight of 5200. The more acidic inhibitor had a PI of 6.5 and contained 39 amino acids with a molecular weight of 4300. Both inhibitors were capable of inhibiting bovine and two human trypsins. They did not inhibit two human chymotrypsins but had a weak capacity to inhibit bovine chymotrypsin.A large body of information has been gathered during the past decade concerning the enzymatic composition of pancreatic juices from various mammalian sources. However, there are only a few reports describing the composition and properties of human pancreatic proteins. This is mainly due to the scarcity of human pancreas and to the difficulties arising from the autolysis of the proteases.Buck et al. Abbreviations. EAhx-Trp-OMe, e-aminocaproyl-mtryptophan methyl ester ; Tos-Arg-OMe, N-p-tosyl-L-argininemethyl ester; Ac-Tyr-OEt, N-acetyl-L-tyrosine ethyl ester; Tos-Phe-CH,CI, ~-l-tosylamido-2-phenylethylchloromethylketone; Tos-Lys-CH,Cl, l-chloro-3-tosylamido-7-amino-2-heptanonc ; Dip-I?, di-isopropylfluorophosphate.Enzymes. Trypsin (EC 3.4.4.4) ; chymotrypsin (EC 3.4.4.5); elastase (ED 3.4.4.7).Definition. A,,, unit, the quantity of material contained in 1 ml of a solution which has an absorbance of 1 a t 280 nm when measured in a 1-cm pathlength -cell.trypsin. Silberberg and Hadron [3] also reported the presence of two chymotrypsin isoenzymes, while Coan and Travis [5,6] found the presence of three forms of chymotrypsin. Differences in the isolation procedures employed, as well as the inherent autodigestabiliby of the pancreatic proteases, seem to be the main reason for these conflicting reports. The work presented here describes a method for the simultaneous isolation of human pancreatic enzymes : trypsin, chymotrypsin and elastase from frozen whole pancreas. The purification schemes were ...

show abstract

“…The results above clearly indicate that Fe2Tf is hydrolyzed by trypsin preferentially at the connecting portion between the N-and C-domains, provided that the proteinase inhibitors present in egg white [6,7] are completely removed from the Tf preparation by CM-and DEAE-chromatography [8] and trypsin is stabilized with Ca2+ [16]. The product of the limited proteolysis is a nicked Fe2Tf in which the two split domains of 35 kDa each are still bound non-covalently.…”

Section: Discussionmentioning

confidence: 85%

“…Apo-Tf, free from trypsin inhibitors [6,7], was prepared in a good yield, (7.3 g from 11 of homogenized hen egg white) according to Yamamura et al [S]. The concentration was determined spectrophotometrically, using A% = 11.3 191.…”

Section: Materials and Methodsmentioning

confidence: 99%

Preparation and characterization of trypsin‐nicked ovotransferrin

et al. 1985

View full text Add to dashboard Cite

The N-and C-domains isolated from ovotransferrin (Tf) with trypsin could be separated from each other and from intact Tf by WPLC with a TX-GEL G-3000SWG-0.1 yO SDS system. The analytical method revealed that Fe {III~-saturated Tf (Fe,Tf) of 77 kDa was hydrolyzed by trypsin Preferentially at the portion connecting both domams. The main product was a nicked Fe,Tf, in which the two fragmented domains of 35 kDa each were still bound together non~ova~ently and showed a notable c~~rativity on their denaturation. Transferrin

show abstract

Physical characterization of ovoinhibitor, a trypsin and chymotrypsin inhibitor from chicken egg white

Cited by 89 publications

References 36 publications

Comparative proteomic analysis of chicken, duck, and quail egg yolks

Comparative proteomic analysis of chicken, duck, and quail egg yolks

Human Pancreatic Proteolytic Enzymes and Protein Inhibitors

Preparation and characterization of trypsin‐nicked ovotransferrin

Contact Info

Product

Resources

About