Secretory form of atrial natriuretic polypeptide as cardiac hormone in humans and rats

1987 ◽  
Vol 65 (8) ◽  
pp. 1756-1761 ◽  
Author(s):  
Kazuwa Nakao ◽  
Akira Sugawara ◽  
Shozo Shiono ◽  
Yoshihiko Saito ◽  
Narito Morii ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Performance Liquid Chromatography ◽  
Coronary Sinus ◽  
Rat Heart ◽  
High Performance ◽  
Low Molecular Weight ◽  
Reverse Phase ◽  
Atrial Natriuretic Polypeptide ◽  
Molecular Weight Form ◽  
Atrial Natriuretic

To elucidate the secretory form of atrial natriuretic polypeptide from the atrium, the molecular form of atrial natriuretic polypeptide in the perfusate from the isolated beating rat heart and in plasma taken at the coronary sinus of 10 patients during cardiac catheterization has been investigated using high performance gel permeation chromatography and reverse phase high performance liquid chromatography coupled with radioimmunoassay for atrial natriuretic polypeptide. Atrial natriuretic polypeptide in the perfusate from the rat heart showed a single peak eluting at the position of a low molecular weight form of atrial natriuretic polypeptide, without any detectable amounts of atrial natriuretic polypeptide with high molecular weights. The major component of atrial natriuretic polypeptide in the rat heart perfusate co-migrated with rat α-atrial natriuretic polypeptide in reverse phase high performance liquid chromatography. In 9 out of 10 patients atrial natriuretic polypeptide in plasma taken at the coronary sinus revealed a single peak of atrial natriuretic polypeptide emerging at the position of human α-atrial natriuretic polypeptide in gel filtration. Only one plasma sample had a small quantity of high molecular weight forms with the predominant low molecular weight form of atrial natriuretic polypeptide. The major component of atrial natriuretic polypeptide in the plasma extract from the coronary sinus was identified with human α-atrial natriuretic polypeptide. These results indicate that α-ANP, a 28-amino acid polypeptide, is secreted as a cardiac hormone into the coronary blood stream from the atrium.

Heterogeneity of antifreeze polypeptides from the Newfoundland winter flounder, Pseudopleuronectes americanus

1984 ◽  
Vol 62 (1) ◽  
pp. 28-33 ◽  
Author(s):  
Ron M. Fourney ◽  
Shashikant B. Joshi ◽  
Ming H. Kao ◽  
Choy L. Hew
Keyword(s):  
Molecular Weight ◽  
High Performance Liquid Chromatography ◽  
Gel Electrophoresis ◽  
High Performance ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Winter Flounder ◽  
Pseudopleuronectes Americanus ◽  
Reverse Phase ◽  
Antifreeze Polypeptides

The heterogeneity of Newfoundland winter flounder antifreeze polypeptides was analyzed by reverse phase high performance liquid chromatography and by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Seven antifreeze polypeptide components could be readily demonstrated. Five of the components were similar in molecular weight (3300) and amino acid composition. Two of the antifreeze polypeptide components were larger (4500) and contained valine. The two major components (components 6 and 8) were identical to those reported earlier from our laboratories.

scholarly journals Determination of 11 Low-Molecular-Weight Carbonyl Compounds in Marine Algae by High-Performance Liquid Chromatography

2006 ◽  
Vol 44 (5) ◽  
pp. 233-238 ◽  
Author(s):  
V. M. da Silva ◽  
M. C. da Cunha Veloso ◽  
E. T. Sousa ◽  
G. Vieira Santos ◽  
M. C. Accioly ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Carbonyl Compounds ◽  
High Performance ◽  
Marine Algae ◽  
Low Molecular Weight

Analysis of enzymatically released peptides by revese-phase high performance liquid chromatography from picomole amounts of apolipoproteins separated on polyacrylamide isoelectric focusing gels

1982 ◽  
Vol 60 (8) ◽  
pp. 790-797 ◽  
Author(s):  
Leo V. Pereira ◽  
Peter J. Dolphin
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Isoelectric Focusing ◽  
High Performance ◽  
Acid Precipitation ◽  
Comprehensive Analysis ◽  
Low Molecular Weight ◽  
Peptide Analysis ◽  
Reverse Phase ◽  
Structural Differences

Methods were developed for the peptide analysis of individual isoproteins of human apolipoproteins separated on urea–polyacrylamide isoelectric focusing (IEF) gels. After IEF the proteins were fixed in the gel matrix by trichloroacetic acid precipitation. Low molecular weight contaminants, including ampholytes, were removed and the proteins were chemically desialylated. Enzymatic digestions with L-1-tosyl-2-phenylethylchloromethyl ketone – trypsin, chymotrypsin, or with thermolysin were accomplished within the gel matrix. The proteolytically released peptides were analyzed by reverse-phase high performance liquid chromatography. These methods facilitated the comprehensive analysis of protein structural differences between individual isoproteins of apolipoproteins in duplicate with as little as 1–2 nmol of each isoprotein, without the use of radiolabels. Human apolipoproteins A-I, C, and E were analysed by these methods.

scholarly journals Searching for Low Molecular Weight Seleno-Compounds in Sprouts by Mass Spectrometry

Molecules ◽  
2020 ◽  
Vol 25 (12) ◽  
pp. 2870 ◽  
Author(s):  
Eliza Kurek ◽  
Magdalena Michalska-Kacymirow ◽  
Anna Konopka ◽  
Olga Kościuczuk ◽  
Anna Tomiak ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Weight ◽  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
High Performance ◽  
Analytical Techniques ◽  
Low Molecular Weight ◽  
Analytical Protocol ◽  
Icp Ms

A fit for purpose analytical protocol was designed towards searching for low molecular weight seleno-compounds in sprouts. Complementary analytical techniques were used to collect information enabling the characterization of selenium speciation. Conceiving the overall characterization of the behavior of selenium, inductively plasma optical mass spectrometry (ICP-MS) was used to determine the total selenium content in entire sprouts as well as in selected extracts or chromatographic fractions. Then, high-performance liquid chromatography combined with ICP-MS (HPLC-ICP-MS) was used to evaluate the presence of inorganic and organic seleno-compounds, with the advantages of being very sensitive towards selenium, but limited by available selenium standard compounds. Finally, ultra-high performance liquid chromatography electrospray ionization triple quadrupole mass spectrometry (UHPLC-ESI-QqQ-MS/MS) and UHPLC-ESI-Orbitrap-MS/MS were used for the confirmation of the identity of selected compounds and identification of several unknown compounds of selenium in vegetable sprouts (sunflower, onion, radish), respectively. Cultivation of plants was designed to supplement sprouts with selenium by using solutions of selenium (IV) at the concentration of 10, 20, 40, and 60 mg/L. The applied methodology allowed to justify that vegetable sprouts metabolize inorganic selenium to a number of organic derivatives, such as seleno-methylselenocysteine (SeMetSeCys), selenomethionine (SeMet), 5′-seleno-adenosine, 2,3-DHP-selenolanthionine, Se-S conjugate of cysteine-selenoglutathione, 2,3-DHP-selenocysteine-cysteine, 2,3-DHP-selenocysteine-cysteinealanine, glutathione-2,3-DHP-selenocysteine, gamma-Glu-MetSeCys or glutamyl-glycinyl-N-2,3-DHP-selenocysteine.

scholarly journals The postnatal methylation of transfer ribonucleic acid in brain. Evidence for the methylation of precursor transfer ribonucleic acid

1979 ◽  
Vol 177 (1) ◽  
pp. 381-384 ◽  
Author(s):  
E Elahi ◽  
O Z Sellinger
Keyword(s):  
Molecular Weight ◽  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Rat Brain ◽  
Ribonucleic Acid ◽  
High Performance ◽  
Low Molecular Weight ◽  
Polyacrylamide Gels ◽  
Cytoplasmic Rna ◽  
Rapid Labeling

Incubation of 3-day-old rat brain with L-[methyl-3H]methionine resulted in the rapid labeling of low-molecular-weight cytoplasmic RNA. Electrophoresis in 15% polyacrylamide gels provided evidence for the methylation of precursor tRNA molecules, and high-performance liquid chromatography demonstrated N2-methylguanine to be the predominant methylated base formed during the first 2 min of labelling.

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