Chemical characterization of the purified component of specific transfer factor in the leukocyte dialysates from HSV-1 immunized goats.
The chemical characterization of the purified component responsible for HSV-1 specific transfer factor activity (PTFC) by high resolution analytical methods was performed. PTFC had a molecular weight of 6,000 dalton by the size-exclusion HPLC analysis; it showed a marked UV-absorbance spot at 254 nm and a fluorescent spot at 366 nm on the thin-layer plate by thin-layer chromatography which spots coincided at the same place of the plate. The amino acid composition and sequencing analyses showed that PTFC consisted of at least twelve different amino acids, but the amino acid sequence could not be determined. The combined results indicate that PTFC is a compound with a molecular weight of 6,000 dalton, composed of peptide and nucleotide-like material. The peptide is rich in aspartic acid and its N-terminal end may be blocked.
Qi
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HY
Department of Biochemistry, Fourth Military Medical University, Xian, Shaan Xi, P.R. China.
Wan
Z F
ZF
Su
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CZ
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002855:Chromatography, Thin Layer; D006041:Goats; D007962:Leukocytes / Q000737:chemistry; D008970:Molecular Weight; D012261:Ribonucleoproteins / Q000737:chemistry*; D018139:Simplexvirus / Q000276:immunology*; D014165:Transfer Factor / Q000737:chemistry*
D000596:Amino Acids; D012261:Ribonucleoproteins; D014165:Transfer Factor