Phenanthrenequinone as an analytical reagent for arginine and other monosubstituted guanidines

Yamada, Shigeki; Itano, Harvey A.

doi:10.1016/0304-4165(66)90256-x

Cited by 459 publications

(113 citation statements)

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“…The plate was developed by ascending chromatography using isopropanoi-acetic acid-water (4: I: I, v/v) (Solvent A) until the solvent reached the top edge of the Abbreviations: Ru B PCase = Ribulose bisphosphate carboxylase, TLC = thin layer chromatography plate. Each sample was spotted on triplicate plates which were stained either with 0.25% ninhydrin in acetone, followed, after bleaching with 2% HC1 in acetone, by the phenanthrenequinone arginine stain (27) and the Pauly reagent for histidine (2) or cadmium ninhydrin (7) followed by 1-nitroso-2-naphthol and HNO 3 as a tyrosine stain (7) or cadmium ninhydrin followed by Ehrlich's reagent for tryptophan (21).…”

Section: Chymotryptic Peptide Mapping Ofmentioning

confidence: 99%

Peptide mapping of the ribulose bisphosphate carboxylase large subunit from the genus Oenothera

Holder

1978

Carlsberg Res. Commun.

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A peptide mapping procedure for the peptides derived by chymotryptic digestion of the large subunit of ribulose-1,5-bisphosphate carboxylase from Oenothera is described. The peptides were characterized first by ion exchange chromatography and then by thin layer chromatography in a number of solvent systems, using ninhydrin and amino acid specific stains for detection. A comparison of the maps from different Oenothera species revealed considerable similarity between the species but with a small number of differences. The results are discussed in relation to the different chloroplast genomes present in Oenothera.

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Section: Chymotryptic Peptide Mapping Ofmentioning

confidence: 99%

Peptide mapping of the ribulose bisphosphate carboxylase large subunit from the genus Oenothera

Holder

1978

Carlsberg Res. Commun.

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“…This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. Amino acid sequence analysis of the fully reduced and alkylated protein (24) was carried out in the automatic sequencer (Beckman 890C) using the Quadrol double cleavage program. Residues released were identified by thin-layer chromatography (25), by back hydrolysis in 6 M HCI under reduced pressure for 24 hr at 1500 followed by amino acid analysis, and by colorimetric assay (His and Arg) (26,27). Three separate determinations made on separately prepared samples, two from milk and one from colostrum, gave equivalent results.…”

mentioning

confidence: 99%

Crystallographic studies of bovine beta2-microglobulin.

Becker¹,

Ziffer²,

Edelman³

et al. 1977

Proc. Natl. Acad. Sci. U.S.A.

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Crystals of the bovine milk protein lactollin yield x-ray diffraction data extending to a resolution of 2.8 A.Lactollin is a bovine analogue of #2-microglobulin, a protein that is homologous in amino acid sequence to the constant domains of immunoglobulins and is the light chain of the human and murine major histocompatability antigens. The protein crystallizes in the orthorhombic space group P212121 with a = 77.4, b = 47.9, and c = 34.3 A. The #2-Microglobulin is a protein distinguished by its similarity to certain portions of immunoglobulins (1-3) and by its association on cell surfaces with the major histocompatability antigens of man (HLA) and mouse (H-2) (4-7). Since its discovery in human urine in 1968, the overall properties, synthesis, and amino acid sequence of this protein have been characterized (2,(8)(9)(10)(11). Similar proteins have been detected in a variety of species, and all appear as a single polypeptide [molecular weight (Mr) = 11,600], with few differences in amino acid sequence among the proteins from different species (2,3,(12)(13)(14).Comparison of the amino acid sequence and other features of human #32-microglobulin with immunoglobulins (1, 15) has indicated that it closely resembles the constant homology regions (16) of immunoglobulins G, M, and E. In intact immunoglobulin molecules, each homology region is closely associated with the corresponding homology region of another immunoglobulin chain in pairs of domains (16, 17), whereas ,62-microglobulin is found associated with the heavy chain of HLA or H-2 antigens or the closely related thymus leukemia antigen (4-7, 18, 19), suggesting that such paired domains may be structural features of these cell surface molecules. In solution,purified Or-microglobulin, however, is generally unpaired; i.e., it appears as a free monomer (8) The elucidation of the three-dimensional structure of ,32-microglobulin would be of particular interest because it would provide an opportunity to compare this molecule in detail with immunoglobulin domains, and thus contribute to an understanding of its interaction with the heavy chains of H-2 and HLA antigens. It has recently been found that lactollin, a crystalline protein isolated from bovine milk and colostrum, has an amino-terminal amino acid sequence sufficiently similar to those of 6B2-microglobulins from several species to indicate that it is probably a bovine homologue of the protein (M. L. Groves, private communication; refs. 20 and 21). Although the reported molecular weight of lactollin is 43,000 (22), it is composed of subunits of 12,000 daltons. We have confirmed the molecular weight of the subunit and the similarity in amino acid sequence to 62-microglobulin. We report here x-ray diffraction studies ofThe costs of publication of this article were defrayed in part by the payment of page charges from funds made available to support the research which is the subject of the article. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. Amino acid sequence ana...

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“…and cadmium-ninhydrin (Heathcote & Washington, 1967). Fluorescamine was used according to Mendez & Lai (1975), the Pauly reagent for histidine and tyrosine according to Dent (1947), phenanthrenequinone for arginine according to Yamada & Itano (1966) and proline was detected with isatin.…”

Section: A P a T E R S O N A N D P H C L A R K Ementioning

confidence: 99%

Molecular Basis of Altered Enzyme Specificities in a Family of Mutant Amidases from Pseudomonas aeruginosa

Paterson

Clarke

1979

Journal of General Microbiology

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A family of mutant amidases has been derived by experimental evolution of the aliphatic amidase of Pseudomonas aeruginosa strain PAC I. Mutation amiEI6, in the structural gene for the enzyme, results in the production of the mutant B amidase by strain B6. This strain, unlike the wild-type, can utilize butyramide for growth. Strain B6 gave rise by a single mutational event to strain V9, utilizing valeramide, and strain PhB3, utilizing phenylacetamide. Strain V9 was not itself able to utilize phenylacetamide but gave rise by mutation to the phenylacetamide-utilizing mutant PhVl. Peptide 108 was isolated from chymotryptic digests of mutant amidases from strains B6, PhB3 and PhV1, but could not be detected in chymotryptic digests of the wild-type amidase. The sequence of peptide 108 was established as Met-Arg-His-Gly-Asp-Ile-Phe. Thermolytic digests of mutant amidases from strains B6, PhB3, PhVl and V9 were compared with digests of the wild-type amidase. A peptide of the composition Met, Arg, His, Gly,, Asp,, Ile, Ser,, Thr, Val was found in the digest of the wild-type amidase and was replaced in the digests of the mutant amidases by a peptide of the composition Met, Arg, His, Gly,, Asp,, Ile, Ser,, Thr, Val, Phe. Mutation amiEl6 is common to the four mutant enzymes and can be accounted for by the mutation Ser -+ Phe. The sequence of the chymotryptic peptide corresponds with the N-terminal sequence of the amidase protein, and can also be related to the thermolysin peptides. It is concluded that mutation amiEl6 is a Ser -+ Phe change at position 7 from the N-terminus and the effect of this on the enzyme conformation is discussed.

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Phenanthrenequinone as an analytical reagent for arginine and other monosubstituted guanidines

Cited by 459 publications

References 4 publications

Peptide mapping of the ribulose bisphosphate carboxylase large subunit from the genus Oenothera

Peptide mapping of the ribulose bisphosphate carboxylase large subunit from the genus Oenothera

Crystallographic studies of bovine beta2-microglobulin.

Molecular Basis of Altered Enzyme Specificities in a Family of Mutant Amidases from Pseudomonas aeruginosa

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