Studies on silk secretion in the trichoptera (F. Limnephilidae)

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Abstract
The ultrastructure and amino acid composition of the secreted silk of two species of trichopteran larvae, Pycnopsyche guttifer (Walk.) and Neophylax concinnus McL., were investigated. The spinnerets of these two animals were also examined by scanning electron microscopy. The silk consists of double-stranded, flat ribbons (1–4 μ wide), composed of bundles of 15–25 Å filaments. There are two components of the silk: the fiber proper and a surrounding coat thought to be a silk “gum”. Only the outer coat is positive to the EM PATP technique of Thiery (1967), which indicated the presence of neutral sugars. Amino acid analyses of Pycnopsyche silk show that, like other silks, two predominant amino acids are glycine and serine. Arginine, unexpectedly, is the third most abundant and there are a large number of basic and long side-chain amino acids. X-ray diffraction studies of the silk indicate that it has a less crystalline, more amorphous structure than that of other silks.

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