Isolation, structure and biological activity of the Trp-containing pentapeptide from uremic fluid

Abiko, Takashi; Onodera, Ikuko; Sekino, Hiroshi

doi:10.1016/0006-291x(79)91851-5

Cited by 33 publications

(15 citation statements)

References 10 publications

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“…Abiko et al [1,2] carried out a systematic study of peptides in dialysis fluids, which give a positive coloration in the Pauly test (revealing histidine), then more recently [3] in Ehrlich's diazo reaction (revealing tyrosine). Thus, after chromatography on Sephadex G15, they found nu merous spots with ninhydrin, but only four spots with the Pauly test; they purposely retained one of these four spots for further purification (Sephadex G 15, then CM Sephadex C25).…”

Section: Methods For the Study And Classification O F M Mmentioning

confidence: 99%

“…Biological fluids were collected from various types of CRF patients, according to the different studies: nondialyzcd patients [14,17,18,24,27,28,41,42,46,[49][50][51]57]; patients dialyzed by different techniques: peritoneal dialy sis [24,28], hemodialysis [1-3,12,14,17,21,24,28,29,31,41, 44.45.50.53.55.57] ; dialyzed patients developing pericar ditis [24,55] or polyneuritis [14,21,24,44]; or CRF pa tients with high levels of creatinine urea [1][2][3]7],…”

Section: Patientsmentioning

confidence: 99%

“…The fluids were often ultrafiltrated on calibrated mem branes before analysis, permitting the elimination of either low-MW substances (Amicon Diaflo UM 05, cutoff: 500 daltons) [1, 3,10,17,29,46] or proteins: Amicon Diaflo PM [24,28]; Millipore Pellicon PSAC (cutoff: 1,000) [14], PSED (cutoff: 25,000) [53]; Rhône-Poulenc AN 69 (cutoff: 20,000) [14,22], polyacrylonitrile (cutoff: 30,000 daltons) [21].…”

Section: Biological Fluidsmentioning

confidence: 99%

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Molecules in the Middle Molecular Weight Range

Contreras¹,

Later²,

Navarro³

et al. 1982

Nephron

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Section: Methods For the Study And Classification O F M Mmentioning

confidence: 99%

Section: Patientsmentioning

confidence: 99%

Section: Biological Fluidsmentioning

confidence: 99%

See 1 more Smart Citation

Molecules in the Middle Molecular Weight Range

Contreras¹,

Later²,

Navarro³

et al. 1982

Nephron

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“…FunckBrentano et al [15] also reported middle molecular weight peptides with a molecular weight range of 1,100-1,300. Abiko et al [16,17] reported the presence of a heptapeptide and a pentapeptide in uremic sera. Zimmerman et al [14] initially characterized peptides with molecular weights of 1,100-1,300, based on calibration of the gel fil tration column.…”

Section: Introductionmentioning

confidence: 99%

Fast Atom Bombardment Mass Spectrometric Determination of the Molecular Weight Range of Uremic Compounds that Displace Phenytoin from Protein Binding: Absence of Midmolecular Uremic Toxins

Dasgupta

Malik

1994

Am J Nephrol

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Uremic compounds are known to displace phenytoin from protein binding, resulting in a higher concentration of the pharmacologically active free fraction of phenytoin. The true chemical identities and molecular weight range of all these compounds are still unknown. We demonstrated that indoxyl sulfate and hippuric acid, which are found at high concentrations in uremic patients, can only partially explain the elevated free phenytoin concentration. Other known uremic compounds, guanidine, methylguanidine, and guanidinosuccinic acid, do not displace phenytoin from the protein-binding sites. Uremic compounds from sera of patients on maintenance hemodialysis were removed using activated charcoal. These compounds were then backextracted from activated charcoal using methanol and analyzed by fast atom bombardment mass spectroscopy. Mass spectra of uremic sera showed no peak over m/z 450, indicating that midmolecular uremic toxins are not involved in displacing phenytoin from protein binding. We also observed additional peaks in the mass spectrum of uremic compounds when compared with the normal serum extract, indicating the presence of several endogeneous compounds in uremic sera, as expected.

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“…Abiko et al [35][36][37] have isolated the tripeptide (His-Gly-Lys), the heptapeptide (His-Pro-Ala-Glu-AsnGly-Lys) and the pentapeptide (Asp-Leu-Trp-Gln-Lys) from the UF of blood obtained from uremic patients. The latter two peptides have been shown to be fragments of plasma proteins.…”

mentioning

confidence: 99%

Medium-Sized Peptides in the Blood of Patients with Uremia

Mabuchi¹,

Nakahashi²

1983

Nephron

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We have carried out high performance liquid chromatographic analysis of serum and ultrafiltrate of blood obtained from uremic patients and normal subjects to elucidate the presence of medium-sized peptides unique to uremia. Many fluorescamine-positive substances, excluding amino acids and guanidine compounds, were increased in uremic serum compared with normal serum. At the 0.5–1.0 pmol/ml serum level, several peaks were unique to uremia. The retention time, fluorescamine reactivity, molecular weight distribution and the result of enzymatic digestion revealed that these peaks are peptidic substances.

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Isolation, structure and biological activity of the Trp-containing pentapeptide from uremic fluid

Cited by 33 publications

References 10 publications

Molecules in the Middle Molecular Weight Range

Molecules in the Middle Molecular Weight Range

Fast Atom Bombardment Mass Spectrometric Determination of the Molecular Weight Range of Uremic Compounds that Displace Phenytoin from Protein Binding: Absence of Midmolecular Uremic Toxins

Medium-Sized Peptides in the Blood of Patients with Uremia

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