Gene Defect of Dermatan Sulfate Proteoglycan of Cattle Affected With a Variant Form of Ehlers-Danlos Syndrome

A defect of the core protein of dermatan sulfate proteoglycan was suspected in a Holstein calf affected with a variant form of Ehlers-Danlos syndrome. The mutation was a guanine-to-adenine transition at nucleotide position 254, which resulted in a serine-to-asparagine substitution of the bovine proteoglycan core protein. This substitution occurred in the serine-glycine dipeptide repeat that was suspected to be the binding portion of dermatan sulfate. This point mutation in the genome was also detected by the use of restriction fragment length polymorphism (RFLP) and polymerase chain reaction (PCR) methods. The results of the RFLP and PCR indicated that the calf was a heterozygote of an abnormal gene and a normal gene of the core protein. The interpretation of these data revealed that the functional abnormality in cutaneous tissues of the calf was caused by an abnormal gene of the proteoglycan core protein, which induced a substitution of amino acid.     

Genome size distribution in phylum Cnidaria

Cnidarians are considered ancestral metazoans and, therefore, are important taxa for studying animal evolution. However, little is known about the group’s genome size (C value), which is an important parameter in whole-genome sequencing. To address this issue, we measured the C values of 27 cnidarian species from Japan, using flow cytometry, and found that they ranged from 0.26 to 3.56 pg. Excluding the results for Agalma elegans and Physalia physalis (order Siphonophorae), which had the highest C values among the species included in the present study, the C values for the cnidarians were 0.26–1.49 pg. In particular, we found that hydrozoans possessed relatively large and wide-ranging C values, indicating that evolution within the group involved considerable gains or losses of genomic content. Overall, the C values reported in the present study could be valuable for whole-genome sequencing, using next-generation sequencers, and for future research in cytogenetics.     

Polyclonal and monoclonal antibodies for the specific detection of the herbicide acifluorfen and related compounds

Polyclonal and monoclonal antibodies reactive with acifluorfen (AF) were prepared by the immunization of, respectively, rabbits and mice with AF-bovine serum albumin conjugates. The reactivities of polyclonal antibody and three monoclonal antibodies (AF 9-1, AF 51-5 and AF 75-144) were examined in an indirect competitive enzyme-linked immunosorbent assay (C-ELISA). The polyclonal antibody reacted with AF at concentrations of 1·5 to 800 μg litre^-1, while the monoclonal antibodies reacted with AF at concentrations of 3 to 24 μg litre^-1 for AF 9-1, 1·5 to 12 μg litre^-1 for AF 51-5 and 12 to 48 μg litre^-1 for AF 75-144. In the presence of up to 40% methanol in C-ELISA, the monoclonal antibodies, particularly AF 75-144, were less affected in their reactivities with AF than was the polyclonal antibody. Moreover AF 9-1 and AF 51-5 specifically reacted with acifluorfen-methyl and oxyfluorfen, while AF 75-144 reacted with chlornitrofen which did not react with the other antibodies. These results indicated that the antibodies are useful for the assay of AF and its related compounds. © 1997 SCI.