Tomoko Hayashi

Silefrin, a sodefrin-like pheromone in the abdominal gland of the sword-tailed newt, Cynops ensicauda

Sodefrin‐like female‐attracting pheromone was purified from the abdominal glands of male sword‐tailed newts, Cynops ensicauda, by gel‐filtration chromatography and reversed‐phase high‐performance liquid chromatography. The final product comprises 10 amino acid residues with the sequence SILSKDAQLK which coincided with the sequence deduced from its precursor cDNA. This peptide was designated silefrin. The sequence of silefrin was different from that of sodefrin by two amino acid residues, with substitutions Leu for Pro and Gln for Leu at positions 3 and 8, respectively. Both native and synthetic silefrin exerted an equipotent activity in attracting conspecific females.

Amino acid sequence around the active site cysteine residue of calcium-activated neutral protease (CANP)

The active site of calcium‐activated neutral protease (CANP) was specifically labeled with iodoacetic acid. The active site hepta peptide was isolated from carboxymethylated CANP after digestion with proteases and the sequence was determined. The sequence indicates that CANP is a thiol protease and its comparison with other thiol proteases is described.

Number and types of peptide chains in thyroglobulin: tryptic peptides of noniodinated hog thyroglobulin

In order to identify the number and types of peptide chains in thyroglobulin, noniodinated 19-S thyroglobulin obtained from goitrogen-treated hogs was exhaustively digested with trypsin (EC 3.4.4.4) after reduction and S-carboxymethylation. The digestion mixture was preliminarily separated into 30 fractions on Sephadex G-100 or G-15 and SE-Sephadex columns. The number of various tryptic peptides contained in each fraction was determined on peptide maps, where spots were detected with ninhydrin for total peptides and with each specific reagent for arginine, histidine or tyrosine-containing peptides. The number of total peptides observed in most of the fractions was estimated to be half the number of lysine plus arginine residues found in each fraction per mole of thyroglobulin, and the number of specific peptides was also close to half the number of each specific amino acid. These findings imply that thyroglobulin has 2-fold symmetry in the structure at the level of tryptic fragments and thus probably at the level of intact peptide chains.

Interprofessional Education Initiatives at Gunma University: Simulated Interprofessional Training for Students of Various Health Science Professions

The School of Health Sciences (the “School”) of the Gunma University has a mandate to train and produce advanced, high-quality health professionals. To enhance collaboration among health professionals and to overcome the fragmented nature of specialized medicine, the School has developed a curriculum based fundamentally on holistic medicine and interprofessional work (IPW). The major advantage of the curriculum lies in its training program-simulated interprofessional training—where students work in groups and undergo a series of activities, including group discussions, clinical training at facilities, general meetings, and reporting. This “teamwork training” is the core subject of the education. Its concept is first shared and discussed during the first year of the curriculum, and training is introduced to the third-year students from all departments of the School. All academic staff help implement the training in cooperation with approximately 20 external health care facilities. The training is evaluated every year, and both students and academic staff have evaluated it positively. This “teamwork training” has been in practice for 9 years now. As medical knowledge has expanded and technology advanced, changes have taken place in IPW at clinical settings. To respond to this, deliberate efforts are being made, including: (1) use of updated case scenarios; (2) participation of students from the School of Medicine; and (3) networking for interprofessional education with external medical facilities and other universities.

The presence of N-terminal pyroglutamyl residues in hog thyroglobulin

A method was devised to isolate N-terminal peptide fragments from the polypeptide chains constituting thyroglobulin even in the case when the terminal amino groups are naturally blocked, for instance, acylated. Reduced and carboxymethylated hog thyroglobulin was first acetylated and digested with thermolysin. The blocked N-terminal peptide fragments were separated from the unblocked N-terminal fragments by column chromatography on Dowex 50, then on Dowex 1 after dinitrophenylation, and finally fractionated into ten fractions by paper chromatography after gel filtration on Sephadex G-10. Structural analyses by enzymic or partial acid hydrolysis of these peptide fractions failed to detect N-terminal acetyl amino acid. Instead, pyroglutamyl peptides including pyroglutamylleucine were found. By the same method, acetylated lysine and glycine were identified for chicken lysozyme and horse myoglobin, respectively. The use of thermolysin because of its unique specificity, and the possible relevance of the present result to the previous data on the N-terminal analysis of thyroglobulin are discussed.