Sensitive identification of the phenylthiohydantoin of arginine

Reed, Roberta G.; Mackay, Carol M.

doi:10.1016/0003-2697(78)90517-1

Cited by 7 publications

(3 citation statements)

References 6 publications

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“…Spots were visualized with fluorescamine (Schütz et al, 1977). pPP itself was not visible with fluorescamine but could be located with phenanthrenequinone (Reed & MacKay, 1978). pPP did not move from the origin.…”

Section: Methodsmentioning

confidence: 85%

Altered amidation of pancreatic polypeptide in cultured dog islet tissue

Paquette¹,

Gingerich²,

Scharp³

1981

Biochemistry

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Three forms of immunoreactive pancreatic polypeptide (PPI) were detected in extracts of cultured dog pancreatic PP cells: PPI of (1) larger apparent molecular weight than PP, (2) similar apparent molecular weight but different isoelectric point than PP, and (3) identical apparent molecular weight and isoelectric point with PP. Dog pancreatic endocrine cells in culture were labeled biosynthetically with tritiated amino acids, and extracted proteins were fractionated by sodium dodecyl sulfate gel electrophoresis. A total of 97% of the PPI migrated like PP itself while about 3% of the PPI migrated like proteins up to 7200 molecular weight. PPI migrating like PP was analyzed further by isoelectric focusing and was found to occur in a neutral form like PP and a more acidic form. Peptide mapping of neutral and acidic PPI forms showed that both were like PP with the exception that the C-terminal [3H]tyrosine-containing peptide was a peptide with a net negative charge of 1 arising from a peptide extension of one or a few amino acids. The acidic form of PP was also shown to occur in pancreas extracts. However, neutral PPI was 90% of the total PPI in the pancreas extracts while the converse was true of culture extracts. We conclude that culturing the PP cell affects the efficiency of the process of amidation, that acidic PP could be either biosynthetic precursor or end product, and that the existence of the larger PP form(s) signals (signal) the possible production of yet other peptides by the PP cell.

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Section: Methodsmentioning

confidence: 85%

Altered amidation of pancreatic polypeptide in cultured dog islet tissue

Paquette¹,

Gingerich²,

Scharp³

1981

Biochemistry

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“…This is shown in Fig. 1, which places it in -Numbers in parentheses code for residue identification by methods as follows: 1, HF'LC; 2, GLC; 3, TLC; 4, dansylation; 5, carboxyterminal analysis (Weise et al, 198Oa); 6, FTH-arginine determination (Reed and MacKay, 1978). The peptides have been found (Weise et al,198Oa) (4.4), isoleucine (0.91, tyrosine (0.6), lysine (3.0), arginine (0.9).…”

Section: Carboxyterminal Sequencementioning

confidence: 99%

Structure of Bovine P₂ Basic Protein: Sequence of a Carboxyterminal Segment That Is a Neuritogen in Rabbits

Hsieh¹,

Weise²,

Levit³

et al. 1981

Journal of Neurochemistry

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The sequence of the carboxyterminal 18 amino acids released by cyanogen bromide digestion of the bovine P2 protein was determined. It has several interesting structural and immunological properties. It contains the only two half-cystines in the molecule that have the capacity to form an intrachain disulfide bond. Using the rabbit as a test animal, this carboxyterminal peptide was capable of producing experimental allergic neuritis. The sequence of this peptide is Val-Val-Glu-Cys-Lys-Met-Lys-Asp-Val-Val-Cys-Thr-Arg-Ile-Tyr-Glu-Lys-Val.

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“…The pH 2.0 buffer was formic acid:acetic acid:water (110 ml: 300 ml: 1,590 ml). Amino acids were detected by spraying with 0.2% ninhydrin in acetone, followed by phenanthrene quinone (36) to detect octopine. Samples recovered for further analysis were eluted from the paper by chromatography with water (recovery of 100%1o), otherwise samples were eluted overnight in scintillation vials in 1 ml 1% acetic acid, 0.1% Triton X-100 and counted in Plasmasol liquid scintillation fluid (46) (recovery 60-70%).…”

mentioning

confidence: 99%