Simultaneous selectivity optimization of mobile and stationary phases in reversed-phased liquid chromatography for isocratic separations of phenylthiohydantoin amino acid derivatives

Glajch, Joseph L.; Gluckman, Jennifer C.; Charikofsky, J.G.; Minor, James M.; Kirkland, J. J.

doi:10.1016/s0021-9673(01)90661-2

Cited by 149 publications

(40 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Amino acid compositions were determined after hydrolysis in 6 M HC1 (24 h at 108°C) using precolumn derivatization with phenylisothiocyanate [16] and reverse-phase chromatography on a Brownlee Ultrasphere ODS column (25 cm × 4.6 mm) using a Waters HPLC system. Peptides and chains were subjected to amino-terminal sequence analysis on a Beckman 890B or 890M se- quencer using polybrene [17], and identifying the PTH amino acids by two different HPLC methods [18,19].…”

Section: Methodsmentioning

confidence: 99%

Collagen type IX: Evidence for covalent linkages to type II collagen in cartilage

et al. 1987

View full text Add to dashboard Cite

A major site of pyridinoline cross-linking in bovine type IX collagen was traced to a tryptic peptide derived from one of the molecule's HMW chains. This peptide gave two amino acid sequences (in 2/1 ratio) consistent with it being a three-chained structure. The major sequence matched exactly that of the C-telopeptide of type II collagen from the same tissue. A second HMW chain that contained pyridinoline cross-links also gave two amino-terminal sequences, one from its own amino terminus, the other matching exactly the Ntelopeptide cross-linking sequence of type II collagen. We conclude that type IX collagen molecules are covalently cross-linked in cartilage to molecules of type II collagen, probably at fibril surfaces.

show abstract

Section: Methodsmentioning

confidence: 99%

Collagen type IX: Evidence for covalent linkages to type II collagen in cartilage

et al. 1987

View full text Add to dashboard Cite

show abstract

“…Sequences were analyzed with a Beckman 890B or 890M sequencer in the presence of polybrene [12] and each phenylthiohydantoin was identified in two different HPLC systems [13][14][15]. Serum with an elevated SAA level, as determined by radioimmunoassay [16], was obtained from a member of a locally maintained flock of Pekin ducks that, 17 months previously, had been injected with a homogenate of amyloidotic duck liver [4].…”

Section: Methodsmentioning

confidence: 99%

Primary structure of duck amyloid protein A The form deposited in tissues may be identical to its serum precursor

et al. 1987

View full text Add to dashboard Cite

The amino acid sequence has been determined for the major protein that accumulates in amyloid fibrils in tissues of the Pekin duck. With the exception of 16 residues at the amino terminus, this 106-residue protein is homologous with human serum amyloid protein A (104-residue apoSAA), which is the putative precursor of the 76-residue protein that accumulates in human patients with amyloidosis. Duck serum is shown to contain a protein that is immunologically related and approximately equal in size (12 kDa) to the deposited form in ducks. These results indicate that proteolytic processing of the precursor is not a necessary step in the deposition of amyloid fibrils, at least in the duck.Amino acid sequence; Amyloid protein A; Amyloidosis; SAA protein; Acute-phase protein; Lipoprotein

show abstract

“…All analyses were performed in the presence of Polybrene@ [ll]. The phenylthiohydantoin derivatives of amino acids were identified by HPLC on a Zorbax CN column (4.6 x 250 mm) with an isocratic system according to the method of Glajch et al [23]. Sequence analyses were also performed with an Applied Biosystems 470A gas-phase sequencer (Foster City, CA), when the available sample was less than 3 nmol.…”

Section: Sequence Analysismentioning

confidence: 99%

Lipopolysaccharide‐sensitive serine‐protease zymogen (factor C) of horseshoe crab hemocytes. Identification and alignment of proteolytic fragments produced during the activation show that it is a novel type of serine protease

Tokunaga

Miyata

Nakamura

et al. 1987

European Journal of Biochemistry

View full text Add to dashboard Cite

The horseshoe crab clotting factor, factor C, present in the hemocytes is a serine-protease zymogen activated with lipopolysaccharide. It is a two-chain glycoprotein ( M r = 123000) composed of a heavy chain ( M , = 80000) and a light chain (Mr = 43000) Eur. J . Biochem. 154, 511 -5211. In our continued study of this zymogen, we have now also found a single-chain form of factor C (Mr = 123000) in the hemocyte lysate. The heavy chain had the NH2-terminal sequence of Ser-Gly-Val-Asp-, consistent with that of the singlechain factor C, indicating that the heavy chain is derived from the NH2-terminal part of the molecule. The light chain had an NH,-terminal sequence of Ser-Ser-Gln-Pro-. Incubation of the two-chain zymogen with lipopolysaccharide resulted in the cleavage of a Phe-Ile bond between residues 72 and 73 of the ligth chain.Concomitant with this cleavage, the A (72 amino acid residues) and B chains derived from the light chain were formed. The complete amino acid sequence of the A chain was determined by automated Edman degradation.The A chain contained a typical segment which is similar in sequence to a family of repeats in human p2-glycoprotein I, complement factors B, protein H, C4b-binding protein, and coagulation factor XI11 b subunit. The NH2-terminal sequence of the B chain was Ile-Trp-Asn-Gly-. This chain contained the serine-active site sequence -Asp-Ala-Cys-Ser-Gly-Asp-SxGl y-Gl y-Pro-.These results indicate that horseshoe crab factor C exists in the hemocytes in a single-chain zymogen form and is converted to an active serine protease by hydrolysis of a specific Phe-Ile peptide bond.The hemocytes circulating in horseshoe crab hemolymph contain a coagulation system, which participates both in hemostasis and in defence against invading microorganisms [l -31. Exposure of the hemocytes to bacterial endotoxins (LPS) results in the activation of the coagulation system, which involves three intracellular serine-protease zymogens. Our recent studies have established that the role of LPS is to induce the activation of zymogen factor C. The active enzyme, factor c, then converts zymogen factor B to its active form factor B, which subsequently activates the proclotting enzyme to clotting enzyme [4-61. This sequential activation of three serine-protease zymogens results in the transformation of coagulogen to insoluble coagulin gel [7 -91. The serine-protease zymogen, factor C, participates in the initial phase of horseshoe crab hemocyte coagulation. It is a two-chain glycoprotein (123 kDa) composed of the 80-kDa heavy chain and the 43-kDa light chain. Upon activation, the light chain is cleaved to form two new fragments, the 8.5-kDa A chain and the 34-kDa B chain, the latter containing a Dip-F-sensitive active site [4]. The activation of factor C, induced by LPS, apparently does not require the presence of any other protease. This makes it an interesting system for further investigation.To learn more about the structure and function of factor C, the present work was undertaken to identify and align the pr...

show abstract

Simultaneous selectivity optimization of mobile and stationary phases in reversed-phased liquid chromatography for isocratic separations of phenylthiohydantoin amino acid derivatives

Cited by 149 publications

References 7 publications

Collagen type IX: Evidence for covalent linkages to type II collagen in cartilage

Collagen type IX: Evidence for covalent linkages to type II collagen in cartilage

Primary structure of duck amyloid protein A The form deposited in tissues may be identical to its serum precursor

Lipopolysaccharide‐sensitive serine‐protease zymogen (factor C) of horseshoe crab hemocytes. Identification and alignment of proteolytic fragments produced during the activation show that it is a novel type of serine protease

Contact Info

Product

Resources

About