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S Levit

Publications and source records attributed to S Levit.

At least 19 recordsLinked to original sources
PubMed1998

Dose distribution for a 32P-impregnated coronary stent: comparison of theoretical calculations and measurements with radiochromic film.

PURPOSE: Restenosis, caused by proliferation of smooth-muscle cells, limits the efficacy of catheter-based revascularization of coronary arteries. Irradiation has been shown to inhibit growth of smooth-muscle cells in vitro and to prevent restenosis in animal models following stent placement. An intraarterial source of 32P, a pure beta emitter with a half-life of 14.28 days and a 90% range in water of 3.6 mm, is almost ideal for irradiating just arterial wall without exposing any other part of the patient's heart or any other organs, while posing minimal hazards to medical personnel. Two types of previously developed coronary stent impregnated with 32P were investigated. This study aimed to calculate and measure the dose outside of two types of 32P-impregnated beta-emitting coronary stents under conditions closely simulating clinical use. METHODS AND MATERIALS: The dose distributions in water surrounding these stents were calculated using a convolution method and measured by exposing radiochromic film in a solid-water phantom. RESULTS: Experimental results were in excellent agreement with theoretical calculations. CONCLUSIONS: Radiochromic dosimetry can be used to measure the dose distribution around a beta-emitting intraarterial stent at distances as small as 0.1 mm from the stent surface. A simple cylindrical shell model is adequate for calculating the dose at points farther than 0.5 mm from the stent surface.

Angioplasty, Balloon, Coronary↗
PubMed1981

Structure of bovine P2 basic protein: sequence of a carboxyterminal segment that is a neuritogen in rabbits.

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.

Amino Acid Sequence↗
PubMed1980

Peptide length requirement for experimental allergic encephalomyelitis in guinea pigs.

Three peptides overlapping the tryptophan region of bovine CNS myelin basic protein were synthesized by the solid phase procedure of Merrifield. These were the nonapeptide H-Phe-Ser-Trp-Gly-Ala-Glu-Gly-Gln-Lys-OH, the octapeptide H-Ser-Trp-Gly-Ala-Glu-Gly-Gln-Lys-OH, and the heptapeptide H-Trp-Gly-Ala-Glu-Gly-Gln-Lys-OH. They were tested for encephalitogenic activity in guinea pigs with either Freund's complete adjuvant containing M. tuberculosis or muramyl dipeptide in incomplete Freund's adjuvant at doses of 10 microgram per animal. The results show that deletion of one or two residues from the amino-terminal end of the nonapeptide destroyed the ability of the shorter peptides to induce clinical but not histological signs of EAE.

Acetylmuramyl-Alanyl-Isoglutamine↗
PubMed1980

Bovine P2 protein: sequence at the NH2-terminal of the protein.

Sequence data from key fragments of the P2 protein established the order of cyanogen bromide (CNBr) peptides in the structure of the protein and the primary structure for approximately one-half of the molecule. Data were obtained from the three tryptic peptides of blocked NH2-terminal CNBr peptide (CN3), the large CNBr peptide of P2 protein (CN1), and a fragment obtained from P2 by cleavage at tryptophan with 2-(2-nitrophenylsulfenyl)-3-methyl-3'-bromoindolenine. This last fragment was found to contain an over-lapping sequence that proved the juxtaposition of CN1 and CN3 in P2 protein. Thus, based on this fact and the characteristics of the CNBr peptides, the P2 structure is composed of CNBr peptides in the order: CN3-CN1-CN2(Val)-CN2(Lys). A comparison was made between the partial sequence of P2 protein and the equivalent portion of the structure of bovine myelin basic protein. The structures of these two proteins were found to be distinctly different although certain similarities are found.

Amino Acid Sequence↗
PubMed1976

Ribonuclease S-peptide. A model for molecular recognition.

The relationship of structure to function in the recognition of ribonuclease S-peptide by S-protein was studied by several methods. Liquid phase peptide synthesis was employed to generate analogs of S-peptide in which from 1 to 8 residues were deleted from the NH2-terminal end of the S-peptide. Additional derivatives were made by substitutions in the NH2-terminal three amino acids or by modifying the S-peptide analogs by trifluoroacetylation. The analogs were generated in the following way. S-Peptide was cleaved with chymotrypsin. The fragment obtained, RNase(9-20), was purified and lengthened step by step using liquid phase peptide synthesis. A second set of analogs were prepared by cleavage of CF3CO-S-peptide with elastase and the resulting CF3CO-RNase(7-20), similarly lengthened. The various analogs of S-peptide were tested in their capacity to combine with S-protein and regenerate biological activity as measured by Vmax and Kb. This work shows a positive contribution of every one of the first 8 NH2-terminal residues of S-peptide to the molecular recognition of S-protein in the presence of RNA substrate. Substitution of the first 3 residues by alanine or blocking of the free amino groups decreases recognition, indicating that the original primary structure is the most favorable one.

Amino Acid Sequence↗