Novel cardiac peptide hormone in several teleosts

To find out the significance of the newest member of the natriuretic peptide family, salmon cardiac peptide (sCP), we have determined the distribution of the peptide and its mRNA as well as the tissue and plasma molecular forms in several teleosts. Using probes based on the salmon sCP cDNA in Northern blot analysis we found mRNA homologous to that of sCP to be present in the heart of 15 fish species representing nine different genera. We developed a specific RIA for the salmon 29 amino acid peptide to be able to study the distribution of the peptide in the heart and plasma of different fish species. Despite the probable interspecies differences in the peptide sequence, large quantities of immunoreactive sCP were found in the atrium, ventricle and plasma of most of the fish species studied, suggesting that a cardiac hormone homologous to sCP has an endocrine function in a large variety of teleost species. The molecular form of the hormone secreted and stored in the tissue was determined by gel filtration high pressure liquid chromatography. In salmon, as in most of the other fish species studied, the predominant immunoreactive sCP in plasma corresponded to the low molecular weight form, with a size similar to that of the biologically active 29 amino acid sCP (sCP-29), whereas the form stored in the heart corresponded to the high molecular weight pro-sCP-sized material. The form secreted by isolated perfused salmon ventricle, in the basal state as well as when mechanically loaded, was the sCP-29-sized peptide, thus ruling out the possibility that the conversion from high to low molecular weight material is caused by plasma proteases. In conclusion, sCP-like peptides are produced and secreted from the heart of a large number of different fish species. Their post-translational processing appears to be remarkably similar to that of mammalian atrial natriuretic peptide.

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Obtaining and estimating the potential of protein nutraceuticals from highly mineralized collagen-containing beef raw materials

Theory and practice of meat processing ◽

10.21323/2414-438x-2021-6-1-10-22 ◽

2021 ◽

Vol 6 (1) ◽

pp. 10-22

Author(s):

N. Yu. Mezenova ◽

S. V. Agafonova ◽

O. Ya. Mezenova ◽

L. S. Baidalinova ◽

T. Grimm

Keyword(s):

Amino Acids ◽

Molecular Weight ◽

Amino Acid ◽

Raw Materials ◽

Water Soluble ◽

Biologically Active ◽

Low Molecular Weight ◽

Enzyme Preparations ◽

Freeze Dried ◽

Mineralized Collagen

Highly mineralized collagen-containing beef raw materials (tibia, fibula and costal bones) are a source of valuable protein nutraceuticals. They include high molecular weight proteins, oligopeptides and amino acids, which anabolic and physiological potential is used insufficiently. Protein nutraceuticals were obtained by high-temperature hydrolysis of beef raw materials in combination with enzymolysis by proteolytic enzyme preparations Alcalase 2,5 L, Protamex, Protosubtilin G3x. The water-soluble fraction of hydrolysates was studied after its separation and freeze-drying on the content of nitrogenous compounds, fats, minerals, formol-titrated nitrogen, fractional molecular composition. The mathematical dependencies of accumulation of low molecular weight products of protein hydrolysis on enzymolysis duration and doses of different enzyme preparations were obtained. The rational technological scheme of complex processing of beef raw materials with production of protein, fat and mineral-protein additives was proposed. The protein weight fraction in the freeze-dried protein hydrolysates was 69.5–89.6%. All studied protein additives contained peptides with a molecular weight of not more than 100 kDa. The content of low-molecular weight oligopeptides with a molecular weight of less than 10 kDa in the protein additives obtained by enzymatic thermal hydrolysis was more than 90%. The amino acid composition of protein additives produced by different hydrolytic methods was analyzed. Sensory and functional-technological properties of freeze-dried protein compositions were studied. The amino acid potential, high assimilability and physiological activity of protein nutraceuticals from collagen-containing beef raw materials were established. It is recommended to use them in the composition of specialized biologically active additives (BAAs) to food of the osteotropic direction in recipes of specialized and personalized products as a source of amino acids and active peptides.

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The complete amino acid sequence of the low molecular weight cytosolic acid phosphatase

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)81649-6 ◽

1989 ◽

Vol 264 (5) ◽

pp. 2560-2567

Author(s):

G Camici ◽

G Manao ◽

G Cappugi ◽

A Modesti ◽

M Stefani ◽

...

Keyword(s):

Molecular Weight ◽

Acid Phosphatase ◽

Amino Acid ◽

Amino Acid Sequence ◽

Low Molecular Weight ◽

Complete Amino Acid Sequence

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Characterisation of Persistent Anti-Xa Activity Following Administration of the Low Molecular Weight Heparin Enoxaparin Sodium (Clexane)

Thrombosis and Haemostasis ◽

10.1055/s-0038-1648852 ◽

1994 ◽

Vol 72 (02) ◽

pp. 275-280 ◽

Cited By ~ 12

Author(s):

David Brieger ◽

Joan Dawes

Keyword(s):

Molecular Weight ◽

Enoxaparin Sodium ◽

Antithrombin Iii ◽

Anticoagulant Activity ◽

Active Material ◽

Biologically Active ◽

Size Exclusion ◽

Low Molecular Weight ◽

Exclusion Chromatography ◽

Liver And Kidney

SummaryIt is widely reported that persistent anti-Xa activity follows administration of low molecular weight heparins. To identify the effectors of this activity we have injected 125I-labelled Enoxaparin sodium into rabbits and subsequently analysed the circulating radiolabelled material and anti-Xa activity by affinity and size exclusion chromatography. Antithrombin III-binding material derived from the injected drug was responsible for all the anti-Xa amidolytic activity. At early times after injection additional anticoagulant activity which was largely attributable to tissue factor pathway inhibitor was measured by the Heptest clotting assay after removal of glycosaminoglycans from plasma samples. Small radiolabelled fragments, including penta/hexasaccharide with affinity for antithrombin III, were detectable in the circulation 1 week later, and sulphated oligosaccharides persisted for 3-4 weeks. Significant quantities of radiolabel remained in the liver and kidney several weeks post-injection; these organs may sequester some of the injected drug and give rise to circulating biologically active material by degradation and secretion of catabolic products into the plasma.

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Characterization of Trypsin Inhibitor in Florunner Peanut Seeds (Arachis hypogaea L.)1

Peanut Science ◽

10.3146/i0095-3679-15-2-10 ◽

1988 ◽

Vol 15 (2) ◽

pp. 81-84 ◽

Cited By ~ 1

Author(s):

E. M. Ahmed ◽

J. A. Applewhite

Keyword(s):

Molecular Weight ◽

Amino Acid ◽

Aspartic Acid ◽

Arachis Hypogaea ◽

Trypsin Inhibitor ◽

Low Molecular Weight ◽

Arachis Hypogaea L ◽

Amino Acid Profiles ◽

Low Levels

Abstract Florunner peanut seeds contained five trypsin isoinhibitors. Amino acid profiles of the trypsin inhibitors fraction showed high levels of aspartic acid, half-cystine and serine and low levels of histidine and tyrosine. The molecular weight of the inhibitor was 8.3 KDa. The presence of multiforms of this inhibitor, its low molecular weight and the high amount of half-cystine indicate that peanut trypsin inhibitor is of the Bowman-Birk type.

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Normal Mature Human Enamel Protein

Journal of Dental Research ◽

10.1177/00220345790580025301 ◽

1979 ◽

Vol 58 (2_suppl) ◽

pp. 986-987 ◽

Cited By ~ 2

Author(s):

A. Belcourt

Keyword(s):

Molecular Weight ◽

Amino Acid ◽

Gel Electrophoresis ◽

Protein Concentration ◽

Polyacrylamide Gel Electrophoresis ◽

Organic Matrix ◽

Low Molecular Weight ◽

Human Enamel ◽

Weak Density ◽

Enamel Protein

Pure enamel was prepared using an original microdissection technic. Protein concentration was 375 μg per gram of enamel. Polyacrylamide gel electrophoresis showed a single fast-migrating zone containing a thin double band. Ultracentrifugation studies suggested that the proteins were of low molecular weight or of weak density. Absorption spectra showed a strong absorbance at 260nm. Amino acid analyses yielded a composition of 25% Gly, 13.5% Glu, 11% Ser, 11% Pro, 2% Cys and 2% Hyp. A glucidic content of 15% was estimated and glucose, galactose, mannose and fucose were identified. The organic matrix of enamel seemed to be constituted of two major glycoproteins probably fibrous but different from keratin.

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