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Biomedical subjects

J M Strottmann

Publications and source records attributed to J M Strottmann.

8 recordsLinked to original sources
PubMed1995

Langerhans cell histiocytosis involving the corpus callosum and cerebellum: gadolinium-enhanced MRI.

Langerhans cell histiocytosis is a systemic disorder consisting of abnormal histiocyte proliferation, in the form of focal deposits. Central nervous system involvement is most common in the hypothalamus, although other sites have been described, such as the cerebellum and the meninges. We present a case with presumed involvement of the corpus callosum and cerebellum, demonstrating gadolinium enhancement on MRI.

Adolescent↗
PubMed1985

Refolding a disulfide dimer of cytochrome c.

A covalent dimer of Saccharomyces cerevisiae iso-1 cytochrome c is stabilized by an interchain disulfide bond involving the cysteine residue penultimate to the C-terminus. The individual chains in the dimer appear to retain the tertiary structural features characteristic for monomeric cytochrome c albeit with some perturbation. The dimer is reversibly denatured by heat, urea, or guanidine hydrochloride in a single cooperative transition whose midpoint is less than that of the monomeric protein. The kinetic profile observed for the refolding of the denatured dimer is characteristic for monomeric cytochromes except for a markedly enhanced slow-phase amplitude.

Circular Dichroism↗
PubMed1984

Spectral studies of horse heart porphyrin cytochrome c.

Removal of the heme iron from cytochrome c to generate porphyrin cytochrome c relieves the quenching of porphyrin fluorescence and enhances the fluorescence of the single tryptophan residue and the 4 tyrosine residues. The intensity of the porphyrin fluorescence is not perturbed by denaturation of the protein at neutral pH using either urea or guanidine hydrochloride. However, the amplitude of tryptophan fluorescence is increased by these denaturants from 5 to about 85% of a model tryptophan residue using solutions of 2 microM tryptophan. In contrast to cytochrome c, the tryptophan fluorescence amplitude of denatured porphyrin cytochrome c is independent of pH over the range pH 3.0 to 7.4. Acidification of solutions of either native or denatured porphyrin cytochrome c markedly alters both the visible absorbance and fluorescence of the protein consistent with protonation of two pyrrole nitrogens on the porphyrin. Preliminary analysis of the spectral changes occurring in the acid transition suggests the presence of an intermediate form having only one of these two pyrrole nitrogens protonated.

Animals↗
PubMed1983

Advantages of preelectrophoretic conjugation of polypeptides with fluorescent dyes.

A rapid simple procedure is described for the conjugation of proteins, glycoproteins, and peptides with the fluorescent dye fluorescein isothiocyanate during the time required to polymerize a polyacrylamide gel. Such conjugation does not perturb the electrophoretic mobility of the polypeptides in detergent containing gels. The location of polypeptide . dye conjugate is evident by inspection immediately upon removal of a gel from an electrophoresis cabinet avoiding the time required for postelectrophoretic staining and destaining procedures. The sensitivity of detection of polypeptide . fluorescein conjugates is at least equivalent to that obtained using Coomassie blue.

Animals↗
PubMed1983

A globular high spin form of ferricytochrome c.

Acidification of a salt-free solution of native low spin globular horse heart ferricytochrome c with HCl causes a single cooperative transition centered at pH 2.5 at 23 degrees C resulting in the formation of denatured high spin ferricytochrome c. By contrast, acidification with HCIO4 uncouples denaturation from the spin-state transition, resulting in the formation of a globular high spin form of ferricytochrome c at pH 0.0 exhibiting only modest conformational differences from native cytochrome c as judged by far ultraviolet circular dichoroic, tryptophan fluorescence, and reduced viscosity measurements. This uncoupling is consistent with the preferential binding of two perchlorate anions to the globular form(s) cytochrome c. The acid spin-state transition of the perchlorate complex is biphasic, having midpoint values at pH 0.7 and 3.6 involving 1.0 and 1.6 protons, respectively, when measured in the presence of 1 M perchlorate.

Animals↗
PubMed1981

Prediction of neutral salt elution profiles for affinity chromatography.

Neutral salts exhibit very marked differences as eluants of proteins from affinity columns. We observe: (i) that the relative potencies of neutral salts as eluants are independent of the protein or the affinity ligand in the systems studied, (ii) that the absolute salt concentration necessary to elute any given protein bound to the affinity matrix is proportional to the algebraic sum of a set of elution coefficients defined herein for the separate ions present in the solution, and (iii) that the proportionality between elution potency and elution coefficient is a function of the affinity of the protein for the immobilized ligand. Given the concentration of one neutral salt required for elution of a protein of interest from an affinity column, the elution capability of any neutral salt at any temperature can be quantitatively predicted for that protein. Accordingly, application and elution protocols for affinity chromatography can be designed to optimize the yield and fold purification of proteins.

Adenosine Triphosphate↗
PubMed1980

Affinity chromatography in nonionic detergent solutions.

Anionic dye affinity chromatography is commonly unproductive in the presence of nonionic detergents used to extract particulate proteins. Using lactate dehydrogenase as a model protein, Cibacron blue F3GA as a model dye, and Triton X-100 as a model detergent, we find that the dye is encapsulated in nonionic detergent micelles, rendering the dye incapable of ligation with the enzyme. However, the dye can be liberatd from the micelles without altering the nonionic detergent concentration by addition of an anionic detergent, such as deoxycholate or sodium dodecyl sulfate, forming mixed anionic/nonionic micelles that displace the anionic dye. Encapsulation of the anionic detergents prevents their activity as protein denaturants. These observations have been successfuly translated to the dye affinity chromatography of a detergent extract of brain particulate cyclic nucleotide phosphodiesterase.

Animals↗