scholarly journals Confirmation of d-aspartic acid in the novel dipeptide β-aspartylglycine isolated from tissue extract of Aplysia kurodai

1989 ◽  
Vol 263 (2) ◽  
pp. 617-620 ◽  
Author(s):  
M Sato ◽  
T Yamaguchi ◽  
N Kanno ◽  
Y Sato
Keyword(s):  
Aspartic Acid ◽  
Body Wall ◽  
Optical Resolution ◽  
Paper Electrophoresis ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Optical Rotatory Dispersion ◽  
The Novel ◽  
Reactive Compound ◽  
High Concentrations

A novel o-phthalaldehyde-reactive compound was found in the h.p.l.c. chromatogram of Aplysia kurodai extract. This compound was isolated by ion-exchange chromatography and preparative high-voltage paper electrophoresis. It was shown by optical-rotatory-dispersion spectrum and optical-resolution h.p.l.c. analysis that this compound consisted of equimolar amounts of D-aspartic acid and glycine. This compound resisted cleavage in the Edman reaction. This peptide was inferred to be beta-D-aspartylglycine, and this was confirmed by synthesis. beta-D-Aspartylglycine was detected in all tissues of Aplysia kurodai, with especially high concentrations in body wall (skin and muscle) and gill.

Post-proline endopeptidase, further characterization of the enzyme from pig kidneys

1984 ◽  
Vol 49 (8) ◽  
pp. 1846-1853 ◽  
Author(s):  
Karel Hauzer ◽  
Tomislav Barth ◽  
Linda Servítová ◽  
Karel Jošt
Keyword(s):  
Amino Acids ◽  
Aspartic Acid ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Relative Molecular Mass ◽  
Enzyme Molecule ◽  
Thiol Compounds ◽  
Modified Method ◽  
N Terminus

A post-proline endopeptidase (EC 3.4.21.26) was isolated from pig kidneys using a modified method described earlier. The enzyme was further purified by ion exchange chromatography on DEAE-Sephacel. The final product contained about 95% of post-proline endopeptidase. The enzyme molecule consisted of one peptide chain with a relative molecular mass of 65 600 to 70 000, containing a large proportion of acidic and alifatic amino acids (glutamic acid, aspartic acid and leucine) and the N-terminus was formed by aspartic acid or asparagine. In order to prevent losses of enzyme activity, thiol compounds has to be added.

Highly concentrated single-chain atomic crystal LiMo3Se3 solution using ion-exchange chromatography

2018 ◽  
Vol 54 (88) ◽  
pp. 12503-12506 ◽  
Author(s):  
Sudong Chae ◽  
Seungbae Oh ◽  
Akhtar J. Siddiqa ◽  
Kyung Hwan Choi ◽  
Weon-Gyu Lee ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Aqueous Solutions ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Single Chain ◽  
Stern Layer ◽  
High Concentrations ◽  
Atomic Crystal

The enlargement of the Stern layer distance caused by this ion exchange improves the dispersibility of (Mo3Se3−)∞ chains and also prevents the re-bundling and aggregation of nanowires in aqueous solutions, even at high concentrations (1 mg mL−1).

scholarly journals Changes in glycosaminoglycan biosynthesis during differentiation in vitro of human monocytes

1983 ◽  
Vol 210 (3) ◽  
pp. 661-667 ◽  
Author(s):  
S O Kolset ◽  
L Kjellén ◽  
R Seljelid ◽  
U Lindahl
Keyword(s):  
Culture Medium ◽  
Negative Charge ◽  
Morphological Changes ◽  
Paper Electrophoresis ◽  
Exchange Chromatography ◽  
Adherent Cells ◽  
The Novel ◽  
Dermatan Sulphate ◽  
Negative Charge Density

Monocytes isolated from human blood were maintained in vitro on plastic culture dishes. After 3-4 days, adherent cells displayed morphological changes previously attributed to differentiation of the cells into histiocytes. 35S-labelled glycosaminoglycans were isolated after incubation of the cells with inorganic [35S]sulphate. Polysaccharide recovered from the culture medium after labelling from day 0 to day 2 or from day 5 to day 7 in vitro was approximately 90% galactosaminoglycan (resistant to deamination by HNO2), irrespective of labelling period. Whereas day-0-2 material was extensively degraded to disaccharide on incubation with the bacterial eliminase chondroitinase AC, a significant portion, about 30%, of the day-5-7 material resisted degradation under the same conditions. The resistant portion was readily depolymerized by treatment with chondroitinase ABC and may be dermatan sulphate. Paper electrophoresis and paper chromatography of the disaccharides obtained by eliminase digestion identified the day-0-2 labelled galactosaminoglycan as chondroitin 4-sulphate. In contrast, the corresponding day-5-7 material yielded approximately 20% disulphated disaccharide, both on digestion with chondroitinase AC and on subsequent enzymic degradation of the chondroitinase AC-resistant fraction. Further treatment of the disulphated disaccharide with chondro-4-sulphatase and chondro-6-sulphatase indicated that both sulphate groups were located on the N-acetylgalactosamine residue. In accordance with these findings, the day-5-7 polysaccharide showed a higher negative charge density than the day-0-2 material on ion-exchange chromatography. It is concluded that the novel properties acquired by the monocyte during prolonged culturing on plastic include the ability to synthesize glycosaminoglycan(s) containing 4,6-disulphated N-acetylgalactosamine units.

The Amino Acid Sequence of Streptomyces griseus Trypsin. II The Tryptic Peptides

1974 ◽  
Vol 52 (5) ◽  
pp. 382-392 ◽  
Author(s):  
L. Jurášek ◽  
L. B. Smillie
Keyword(s):  
Soluble Fraction ◽  
Streptomyces Griseus ◽  
Paper Electrophoresis ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Insoluble Residue ◽  
Limited Extent ◽  
Terminal Sequence ◽  
Tryptic Peptides ◽  
Final Purification

Streptomyces griseus trypsin (S.G.T.) isolated from pronase was reduced, aminoethylated, and digested with trypsin. The soluble peptides were recovered and the insoluble residue redigested with chymotrypsin. Following recovery of the soluble fraction, the insoluble portion was in turn digested with α-lytic protease of Myxobacter 495. The three groups of soluble peptides were separately subjected to ion-exchange chromatography on the Technicon peptide analyzer and to final purification by high-voltage paper electrophoresis. Sequence analysis by the dansyl-Edman procedure provided unique sequences from the soluble tryptic peptides accounting for 65% of the S.G.T. molecule. Peptides obtained from the redigests of the insoluble residues accounted for an additional 20%.Tryptic digestion of dansylated S.G.T. yielded a unique α-NH2 dansylated peptide whose composition showed it to be the same as the NH2-terminal sequence previously postulated for this enzyme. The tryptic peptides isolated in this work have provided overlaps for many of the previously sequenced peptic peptides. Three continuous sequences of 49, 36, and 28 residues have been elucidated.Evidence has also been obtained that the NH2-terminal valine residue was, to a limited extent, aminoethylated during reaction of the reduced protein with ethylenimine.

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