Abstract
This chapter explores a possible structure of slow-reacting substance of anaphylaxis (SRS-A) that can be hydrolyzed and inactivated by purified human placental arylsulfatase (AS) B. Arylsulfatase B is used for the analysis of degradation products from SRS-A. The amino acid composition of SRS-A is determined after hydrochloric acid (HCL) degradation. Analysis of the hydrazine degradation products by thin layer chromatography (TLC) revealed the presence of glycine and glutamic acid. Dinitrophenylglutamic acid was identified in the analysis of HCL degradation products of dinitrophenylated SRS-A by TLC. These data demonstrated that the substituent at C-6 eicosatetraenoic acid consisted of three amino acids, viz. cysteic acid or its derivative, glutamic acid as the N-terminal residue, and glycine as the C-terminal residue. In order to examine the substrate specificity of purified human placental arylsulfatase B, 500 units of SRS-A in 0.2 M acetate buffer at pH 5.7 was incubated with 750 units of ASA or 300 units of ASB at 37 ° for 90 min, and then the residual contractile activity of SRS-A was determined.
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