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Eight field trials were conducted in 1989 and 1990 in Georgia (USA) and Maryland (USA) to evaluate baits and baiting strategies for delivering oral rabies vaccines to raccoons (Procyon lotor). Bait packets consisting of corn meal and egg batter-based baits enclosed in plastic bags were placed at 1.0-m diameter, raked tracking stations and checked daily. Packets were well accepted by raccoons; they visited 31 to 44% of the tracking stations where they removed 69 to 90% of the packets within 4 to 5 days. All or nearly all baits were removed from plastic bags and less than 1% of the baits were found only partially eaten. No rejection of water-filled paraffin ampules in baits was observed. The use of an odor attractant on bait packets did not appear to enhance bait discovery when packets were placed on raccoon travel routes. An attractant did enhance discovery when baits were placed off-road in a simulated aerial baiting test. Nontarget species comprised 31 to 53% of all visits to the stations; they took 28 to 55% of the baits but did not appear to adversely affect bait availability for raccoons. A total of 2,300 baits, each containing a wax ampule holding 10 mg of a physiological marker (iophenoxic acid), were distributed at a rate of 82 baits/km2 on 2,800 ha of Sapelo Island, Georgia. Thirty-five (65%) of 54 raccoons collected following bait placement had eaten one or more baits as indicated by elevated levels of iodine in the blood serum.

Capillaria hepatica infection was diagnosed by histologic examination in 21 of 71 (30%) coyotes in Louisiana. All infected coyotes were at least 1 year old, and most (19 of 21) were more than 2 year years old. Capillaria hepatica was not found in any livers from 31 red foxes and 20 gray foxes examined.

Cabbage (Brassica oleracea var capitata) leaves were used as a source of cystine lyase. Diethylaminoethyl-cellulose chromatography resolved two peaks of activity, designated I and II.Cystine lyase I (molecular weight 145,000) and O-acetylserine sulfhydrylase (molecular weight 70,000) were resolved by Bio-Gel A-0.5M chromatography. This isozyme catalyzed an alpha,beta-elimination reaction with cystine, cysteine, O-acetylserine, and several S-substituted cysteines. The substrate specificity was similar to previously reported S-alkylcysteine lyases. The elution profiles during purification, and heat inactivation studies indicated that the above reactions were catalyzed by a single protein. The pH optimun with cystine and cysteine as substrate was 8.5 to 9.0, and the K(m) values were: cystine (0.3 mm), cysteine (0.3 mm), O-acetylserine (6 mm), and S-methylcysteine sulfoxide (1.8 mm).Cystine lyase II was resolved into three peaks (molecular weight greater than 500,000, 240,000, and 145,000) using Bio-Gel A-0.5M chromatography. This enzyme degraded l-cystine, l-cysteine, O-acetylserine, S-methylcysteine sulfoxide, and djenkolic acid. The pH optimum with cystine and cysteine was 8.5 to 9.0, and the K(m) values were: cystine (0.3 mm), cysteine (0.3 mm), O-acetylserine (12.5 mm), and S-methylcysteine sulfoxide (3.7 mm).