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Biomedical subjects

R K Brown

Publications and source records attributed to R K Brown.

8 recordsLinked to original sources

The broken wire suture.

The body is a hostile environment for wire sutures. Although the problems of electrochemical corrosion, direct chemical attack on the suture, and inflammation produced in reaction to the suture have been largley eliminated by the use of austenitic stainless steel wires, failure of the wires may still occur due to mechano-chemical cracking -- the combined effect of insignificant stresses, usually from cold working, and insignificant chemical potentials produced by body fluids. Although stainless steel wire remains a satisfactory material for sternotomy closure or for reattaching costal cartilages, the two spectacular complications of a broken wire point out the need for care in using wire sutures. Bending, twisting, kinking and knotting must be avoided as much as possible.

Adult

Pharmacokinetics of the absorption, distribution, and elimination of melphalan in the dog.

[14C]melphalan ([14C]L-PAM) was rapidly absorbed from the gut of dogs after oral dosing and reached a maximum concentration in the serum by 30 minutes. The disappearance of L-PAM (intact drug) from the serum was biphasic after iv administration, with half-lives of 14 and 66 minutes for the alpha and beta phases, respectively. The urinary excretion accounted for 44% of the total radioactivity and 25% appeared in the feces. Approximately 8% of the dose was excreted unchanged in the urine. Biliary excretion was rapid, with 11% of the dose being accounted for in the bile after 30 minutes; approximately 80% of these drug equivalents (materials containing radioactivity) was parent compound. Since large amounts of L-PAM appeared in the bile, the agent may prove to be active against cancers of the gall bladder, bile ducts, and duodenum.

Animals

Multiple antigenic sites on an eicosapeptide. I. Precipitin studies in the goat.

Purified peptide 105-124, an antigenic determinant from the carboxy terminus ribonuclease, was found to form an immune precipitate with antibody to that region prepared by affinity chromatography from goat hyperimmune antiserum to reduced carboxymethylated ribonuclease (CM-RNase). Cm-rnase also gave an immune precipitate with the antibody. Purified antibody to another region of similar size (40-61) did not form a precipitate with CM-RNase but did co-precipitate in the presence of antibody to peptide 105-124 and CM-RNase. The precipitin reaction between antibody to peptide 105-124 and CM-RNase was inhibited by two synthetic derivatives, peptides 118-124 and ala114-RNase 114-124. Stoichiometry of the precipitin reactions of antibody to 105-124 with CM-RNase or peptide 105-124 suggested an antigen valency of three or more. Consistent with this both peptides 105-124 and ala114-RNase 114-124 elicited immediate cutaneous reactions but 118-124 did not. These findings suggest that the eicosapeptide 105-124 is multivalent since at least three antibodies can react simultaneously with it.

Animals

A method for the measurement of L-phenylalanine mustard in the mouse and dog by high-pressure liquid chromatography.

The distribution of L-phenylalanine mustard (L-PAM) was studied in dogs and mice by high-pressure liquid chromatography. Separation of L-PAM from its products of hydrolysis was accomplished with a mu-Bondapak C18 column, a solvent system composed of 2-methoxyethanol/0.1% acetic acid, and solvent programming with a step gradient. Complete separation was effected in less than 15 min. The half-life for disappearance of L-PAM from mouse blood was 41 min, whereas that from dog blood was 29 min. The monohydroxy derivative of L-PAM, L-MOH, disappeared from dog serum with a half-life of 32 min. L-MOH was not detectable in mouse tissue other than blood at times greater than 15 min after injection. In the dog at 4 hr after injection, the tissue/serum concentration ratios were greater than 1 for liver, spleen, intestine, skeletal muscle, urinary bladder and gallbladder. The concentration of L-PAM in the bile was approximately 500 times higher than that in serum.

Animals