. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. RICHARD E. SHORE TABLE I Mole per . cut composition of axial filament protein Residue Molf ' Residue Molr'; Mole% Residue Mole% Asp/ 'Asa 14 Ala Pro His Glv 11 Ser Phe Arg Val 10 Leu Lys Tyr Glu/Gln q [le Cys Thr Mel (1951) on | of this filter gave a color equivalent to 900 /z,g protein. That indi- cates the presence of about mg protein in the mg residue for about 29% protein. This nig residue had the characteristic lavender color we have noted before
. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. RICHARD E. SHORE TABLE I Mole per . cut composition of axial filament protein Residue Molf ' Residue Molr'; Mole% Residue Mole% Asp/ 'Asa 14 Ala Pro His Glv 11 Ser Phe Arg Val 10 Leu Lys Tyr Glu/Gln q [le Cys Thr Mel (1951) on | of this filter gave a color equivalent to 900 /z,g protein. That indi- cates the presence of about mg protein in the mg residue for about 29% protein. This nig residue had the characteristic lavender color we have noted before in preparations of spicule residue. In HF or upon drying from HF, the residue is lavender. \Yater washing changes the color reversibly to a straw tan. The results of the determinations of amino acid composition are summarized in Table I. \Yhen the initial separations were made using the Lowry value for protein content, the- quant it \ of amino acids recovered was so far below that estimated that the chromatograph could not be used for a quantitative indica- tion of the amino acid composition. A pair of determinations was then made using larger quantities of material. The most reliable estimate of the values for methionine and cysteine are believed to be those based on the pre-oxidized sample from which methionine is recovered as the sulfon and cysteine as cysteic acid. The paired values to other amino acids are within one mole per cent of each other. except as expected for methionine and cysteine. The major components of axial filament protein are aspartic (including asparagine), glycine. valine, and glutamic (including glutamine). There is no detectible hydroxyproline or hydroxylysine. Tryptophane would have been destroyed by the hydrolysis so it remains totally tin- FIGURE 6. Time course of 3H-leucine incorporation into bulk protein for fingerlets of Hyinciiiacidon Please note that these images are extracted from scanned page images
Size: 1567px × 1594px
Photo credit: © Library Book Collection / Alamy / Afripics
License: Licensed
Model Released: No
Keywords: ., bookauthorlilliefrankrat, booksubjectbiology, booksubjectzoology
