-
International Journal of Peptide and... Mar 1982The development of, and findings in, a long-term research program on penguin proteins and polar fish blood proteins are described. Two of the egg-white proteins from the... (Review)
Review
The development of, and findings in, a long-term research program on penguin proteins and polar fish blood proteins are described. Two of the egg-white proteins from the Adelie penguin (Pygoscelis adeliae) have unique properties: a glycoprotein named penalbumin that is a major constituent with some characteristics similar to ovalbumin, and an ovomucoid with strong inhibitory capacity for subtilisin as well as for bovine trypsin and alpha-chymotrypsin. The antifreeze glycoproteins from Antarctic fish (Trematomus borchgrevinki and Dissostichus mawsoni) and an Arctic fish (Boreogadus saida) appear to function noncolligatively by lowering the freezing temperature without affecting the melting point. Current evidence indicates that the antifreeze glycoprotein functions at the ice-solution interface, either on the ice surface or in a transition layer between the solution and the ice.
Topics: Animals; Antarctic Regions; Antifreeze Proteins; Arctic Regions; Biological Evolution; Birds; Blood Proteins; Cold Climate; Egg Proteins; Egg White; Female; Fishes; Freezing; Glycoproteins; Ovomucin; Species Specificity
PubMed: 6749729
DOI: 10.1111/j.1399-3011.1982.tb03030.x -
Food Chemistry Sep 2017The effect of pH (4, 5, 7, and 9) combined with either heat (60, 80°C for 10min) or pulsed electric fields (PEF) (1.4-1.8kV/cm, 260-690kJ/kg) treatments on the in vitro...
The effect of pH (4, 5, 7, and 9) combined with either heat (60, 80°C for 10min) or pulsed electric fields (PEF) (1.4-1.8kV/cm, 260-690kJ/kg) treatments on the in vitro peptic digestion of ovomucin-depleted egg white was investigated. Protein digestibility, unaffected by 60°C heating, was increased by heating at 80°C, which caused protein aggregation and solution turbidity. Compared to ovalbumin and lysozyme, ovotransferrin was more susceptible to pepsinolysis. Susceptibility to pepsinolysis of ovalbumin and lysozyme was markedly enhanced by heating at 80°C, compared to either 60°C heating or PEF processing. MALDI-MS identified proteolytic fragments from ovalbumin and lysozyme, exhibiting varied resistance to pepsinolysis. PEF processing at ∼690kJ/kg and pH 4 increased protein digestibility to a similar level to that obtained after heating at 80°C, with negligible solution turbidity, showing potential for the production of digestible protein drinks with good consumer visual appeal owing to their clarity.
Topics: Conalbumin; Egg White; Hot Temperature; Hydrogen-Ion Concentration; Ovomucin; Temperature
PubMed: 28449993
DOI: 10.1016/j.foodchem.2017.03.136 -
British Journal of Experimental... Feb 1951
Topics: Mucins; Orthomyxoviridae; Ovomucin
PubMed: 14821248
DOI: No ID Found -
Journal of Chromatography. A Aug 1994An improved procedure is described involving gel permeation and anion-exchange chromatography for the purification of four major hen egg white proteins. The procedure...
An improved procedure is described involving gel permeation and anion-exchange chromatography for the purification of four major hen egg white proteins. The procedure involves a first-step purification of ovomucin and lysozyme by gel permeation on a Superose 6 Prep Grade column. In the second step, anion-exchange chromatography on Q Sepharose Fast Flow led to the isolation of ovotransferrin and ovalbumin from a gel permeation chromatographic peak. The purities were estimated as ca. 80, 100, 80 and 100% for ovomucin, lysozyme, ovotransferrin and ovalbumin, respectively. The purification yield was over 60% for each protein. Further characterization of purified lysozyme revealed that it was fully active and homogeneous in relation to the electrospray ionization mass spectrum. The electrospray ionization mass spectrum showed different ovotransferrin species. The amino acid composition of purified ovomucin was compared to those published previously.
Topics: Amino Acids; Animals; Chickens; Chromatography, Gel; Chromatography, Ion Exchange; Conalbumin; Egg White; Female; Mass Spectrometry; Muramidase; Ovalbumin; Ovomucin
PubMed: 7921188
DOI: 10.1016/0021-9673(94)80156-8 -
DNA Sequence : the Journal of DNA... Aug 2004The primary amino acid sequence of alpha-subunit in ovomucin (OVM) from hen thick egg white was determined. The 2087 amino acid residues with a relative molecular mass...
The primary amino acid sequence of alpha-subunit in ovomucin (OVM) from hen thick egg white was determined. The 2087 amino acid residues with a relative molecular mass of 230.9 kDa along the full length of the alpha-subunit were represented. The alpha-subunit contains domains, arranged from the N- to C-terminals in the following order: D1-D2-D'-D3-R (central region)-D4-C1-CK (Cystine-knot), in a manner similar to the arrangement of D, C and CK domains in human pre-pro-von Willebrand factor (hpp-vWF) and hMUC2. The alpha-subunit showed identities on amino acid sequences with hpp-vWF and hMUC2 at 33 and 41% in the N-terminal region and 30 and 38% in the C-terminal region, respectively. The numbers and positions of cysteine residues were highly conserved among alpha-subunit, hpp-vWF and hMUC2. However, R showed no virtual sequence homology with the corresponding regions in two proteins. It was estimated that alpha-subunit was not part of a large peptide of OVM, but was independently synthesized from beta-subunit.
Topics: Amino Acid Sequence; Animals; Base Sequence; Blotting, Northern; Chickens; DNA, Complementary; Molecular Sequence Data; Ovomucin; Sequence Analysis, Protein
PubMed: 15620212
DOI: 10.1080/10425170410001723921 -
Biochimie Jan 1992Four hundred MHz 1H-NMR and 100 MHz 13C-NMR spectra of thirteen sialylated oligosaccharide-alditols isolated from hen ovomucin and swallow nests (Collocalia mucin) were...
Four hundred MHz 1H-NMR and 100 MHz 13C-NMR spectra of thirteen sialylated oligosaccharide-alditols isolated from hen ovomucin and swallow nests (Collocalia mucin) were studied. The resonance assignments were determined by combining multiple-relayed coherence-transfer chemical-shift-correlated spectroscopy (multiple-Relay-Cosy) and 1H/13C chemical-shift-correlated 2-D experiments.
Topics: Animals; Birds; Carbon Isotopes; Chickens; Magnetic Resonance Spectroscopy; Mucins; Oligosaccharides; Ovomucin; Tritium
PubMed: 1576207
DOI: 10.1016/0300-9084(92)90182-e -
Applied Microbiology and Biotechnology Feb 2016The biosynthesis of secondary metabolites in fungi is catalyzed by enzymes encoded by genes linked in clusters that are frequently co-regulated at the transcriptional... (Review)
Review
The biosynthesis of secondary metabolites in fungi is catalyzed by enzymes encoded by genes linked in clusters that are frequently co-regulated at the transcriptional level. Formation of gene clusters may take place by de novo assembly of genes recruited from other cellular functions, but also novel gene clusters are formed by reorganization of progenitor clusters and are distributed by horizontal gene transfer. This article reviews (i) the published information on the roquefortine/meleagrin/neoxaline gene clusters of Penicillium chrysogenum (Penicillium rubens) and the short roquefortine cluster of Penicillium roqueforti, and (ii) the correlation of the genes present in those clusters with the enzymes and metabolites derived from these pathways. The P. chrysogenum roq/mel cluster consists of seven genes and includes a gene (roqT) encoding a 12-TMS transporter protein of the MFS family. Interestingly, the orthologous P. roquefortine gene cluster has only four genes and the roqT gene is present as a residual pseudogene that encodes only small peptides. Two of the genes present in the central region of the P. chrysogenum roq/mel cluster have been lost during the evolutionary formation of the short cluster and the order of the structural genes in the cluster has been rearranged. The two lost genes encode a N1 atom hydroxylase (nox) and a roquefortine scaffold-reorganizing oxygenase (sro). As a consequence P. roqueforti has lost the ability to convert the roquefortine-type carbon skeleton to the glandicoline/meleagrin-type scaffold and is unable to produce glandicoline B, meleagrin and neoxaline. The loss of this genetic information is not recent and occurred probably millions of years ago when a progenitor Penicillium strain got adapted to life in a few rich habitats such as cheese, fermented cereal grains or silage. P. roqueforti may be considered as a "domesticated" variant of a progenitor common to contemporary P. chrysogenum and related Penicillia.
Topics: Alkaloids; Evolution, Molecular; Gene Rearrangement; Heterocyclic Compounds, 4 or More Rings; Indoles; Metabolic Networks and Pathways; Multigene Family; Ovomucin; Penicillium; Piperazines
PubMed: 26668029
DOI: 10.1007/s00253-015-7192-y -
The Australian Journal of Experimental... May 1949
Topics: Cholera; Humans; Mucins; Ovomucin; Vibrio; Vibrio cholerae
PubMed: 18137175
DOI: 10.1038/icb.1949.25 -
Biochimica Et Biophysica Acta Mar 2000Proteinases perform many beneficial functions that are essential to life, but they are also dangerous and must be controlled. Here we focus on one of the control... (Comparative Study)
Comparative Study Review
Proteinases perform many beneficial functions that are essential to life, but they are also dangerous and must be controlled. Here we focus on one of the control mechanisms: the ubiquitous presence of protein proteinase inhibitors. We deal only with a subset of these: the standard mechanism, canonical protein inhibitors of serine proteinases. Each of the inhibitory domains of such inhibitors has one reactive site peptide bond, which serves all the cognate enzymes as a substrate. The reactive site peptide bond is in a combining loop which has an identical conformation in all inhibitors and in all enzyme-inhibitor complexes. There are at least 18 families of such inhibitors. They all share the conformation of the combining loops but each has its own global three-dimensional structure. Many three-dimensional structures of enzyme-inhibitor complexes were determined. They are frequently used to predict the conformation of substrates in very short-lived enzyme-substrate transition state complexes. Turkey ovomucoid third domain and eglin c have a Leu residue at P(1). In complexes with chymotrypsin, these P(1) Leu residues assume the same conformation. The relative free energies of binding of P(1) Leu (relative to either P(1) Gly or P(1) Ala) are within experimental error, the same for complexes of turkey ovomucoid third domain, eglin c, P(1) Leu variant of bovine pancreatic trypsin inhibitor and of a substrate with chymotrypsin. Therefore, the P(1) Leu conformation in transition state complexes is predictable. In contrast, the conformation of P(1) Lys(+) is strikingly different in the complexes of Lys(18) turkey ovomucoid third domain and of bovine pancreatic trypsin inhibitor with chymotrypsin. The relative free energies of binding are also quite different. Yet, the relative free energies of binding are nearly identical for Lys(+) in turkey ovomucoid third domain and in a substrate, thus allowing us to know the structure of the latter. Similar reasoning is applied to a few other systems.
Topics: Amino Acid Sequence; Animals; Binding Sites; Endopeptidases; Enzyme Activation; Enzyme Precursors; Humans; Models, Molecular; Molecular Sequence Data; Ovomucin; Protease Inhibitors; Protein Conformation; Proteins; Serine Proteinase Inhibitors; Substrate Specificity; Thermodynamics
PubMed: 10708867
DOI: 10.1016/s0167-4838(99)00284-8 -
Methods in Molecular Biology (Clifton,... 2002
Topics: Animals; Calorimetry, Differential Scanning; Chickens; Ovomucin; Protein Denaturation; Protein Folding; Thermodynamics; Ubiquitin
PubMed: 11859754
DOI: 10.1385/1-59259-184-1:113