[48] Solid-phase peptide synthesis

Doscher, Marilynn S.

doi:10.1016/0076-6879(77)47050-2

Cited by 10 publications

(4 citation statements)

References 142 publications

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“…Figure 10. Fluorescence spectra of isomolar concentrations (8.9 X 1CT7 M) of Boc-tryptophylcasein (-•-) and tryptophylcasein (-)• peptides in homogeneous solution or solid phase peptide synthesis (Merrifield, 1969;Fridkin and Patchornik, 1974; Katsoyannis and Schwartz, 1977;Doscher, 1977). Among these are two different methods in which the amino group responsible for the nucleophilic attack of an activated carboxyl group is the amino group of a protein.…”

Section: Discussionmentioning

confidence: 99%

Covalent attachment of amino acids to casein. 1. Chemical modification and rates of in vitro enzymic hydrolysis of derivatives

Puigserver¹,

Sen²,

Gonzales-Flores³

et al. 1979

J. Agric. Food Chem.

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Section: Discussionmentioning

confidence: 99%

Covalent attachment of amino acids to casein. 1. Chemical modification and rates of in vitro enzymic hydrolysis of derivatives

Puigserver¹,

Sen²,

Gonzales-Flores³

et al. 1979

J. Agric. Food Chem.

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“…The peptides were synthesized by the solid-phase method of Merrifield as described by Doscher (10). In each case, a solid white powder was obtained with a recovery of 40 mg of P-I and 50 mg of P-II.…”

Section: Methodsmentioning

confidence: 99%

Reaction of staphylococcal alpha-toxin with peptide-induced antibodies

et al. 1989

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Two peptides representing separate 13-amino-acid sequences of staphylococcal alpha-toxin have been synthesized and acrylamide gel-purified alpha-toxin monomer and hexamer forms have been prepared and used to produce antisera in rabbits. We report here that each synthetic peptide, P-I and P-II, induces the formation of a specific precipitating antiserum. Moreover, these sera also react with the toxin monomer and sometimes with the hexamer, indicating that each peptide has more than one epitope. The purified toxin monomer can induce antibodies to fragments of toxin but is significantly less potent than the hexamer in inducing antibodies to the toxin monomer and almost not effective in inducing a response to the toxin hexamer. The purified toxin hexamer induces responses that are almost the reciprocals of the monomers, with the antihexamer and-monomer responses dominating and almost no responses to fragments of toxin being induced. These responses are interpreted in terms of the stability of the toxin hexamer to proteolytic degradation, compared with the relative sensitivity of the monomer to proteases. In assays of toxinneutralization activity, only those sera containing antihexamer antibodies can block toxin hemolytic activity. This is true for both peptideand toxin-induced antisera. The basis for this apparent association between

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“…Synthesis of RNase 111-124. RNase 111-124, first synthesized by Lin et al (1970), was prepared by use of solidphase peptide synthetic methods (Merrifield, 1963;Doscher, 1977; Barany & Merrifield, 1979). Commercial chloromethylated poly(styrene-co-l% divinylbenzene) resin (Lab Systems, Inc., lot PMR-16G, 0.74 mmol of Cl/g) was converted to the corresponding hydroxymethylated derivative according to published methods (Gisin & Merrifield, 1972;Wang, 1975).…”

Section: Methodsmentioning

confidence: 99%

Characterization of the histidine proton nuclear magnetic resonances of a semisynthetic ribonuclease

Doscher¹,

Martin²,

Edwards³

1983

Biochemistry

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The proton magnetic resonance spectrum at 300 MHz of the histidine residues in a semisynthetic derivative of bovine pancreatic ribonuclease (RNase A) has been determined. The derivative RNase 1-118 . 111-124 was prepared by enzymically removing six residues from the COOH terminus of the protein (positions 119-124) and then complementing the inactive RNase 1-118 with a chemically synthesized peptide containing the COOH-terminal 14 residues of ribonuclease (RNase 111-124) [Lin, M.C., Gutte, B., Moore, S., & Merrifield, R.B. (1970) J. Biol. Chem. 245, 5169-5170]. Comparison of the line positions of the C(2)-1H resonances of these residues and of their pH dependence with those reported by other workers has allowed assignment of the resonances to individual residues, as well as the determination of individual pK values for histidine-12, histidine-105, and histidine-119. The assignment of histidine-119 was confirmed by the use of a selectively deuterated derivative. The titration behavior of all four histidine residues is indistinguishable from that observed by others for bovine pancreatic ribonuclease A. Partial dissociation of the noncovalent semisynthetic complex was evident at 30 degrees C, pH 4.0, 0.3 M NaCl; pertinent spectra were analyzed to provide an estimate of the association constant between the component chains under these conditions of 1.9 X 10(3) M-1.

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[48] Solid-phase peptide synthesis

Cited by 10 publications

References 142 publications

Covalent attachment of amino acids to casein. 1. Chemical modification and rates of in vitro enzymic hydrolysis of derivatives

Covalent attachment of amino acids to casein. 1. Chemical modification and rates of in vitro enzymic hydrolysis of derivatives

Reaction of staphylococcal alpha-toxin with peptide-induced antibodies

Characterization of the histidine proton nuclear magnetic resonances of a semisynthetic ribonuclease

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