Are the arginine kinase isoenzymes ofLimulus polyphemusthe product of two separate genes?

✍ Scribed by Sandra L. Blethen

• Book ID: 104784919
• Publisher: Springer
• Year: 1971
• Tongue: English
• Weight: 702 KB
• Volume: 5
• Category: Article
• ISSN: 0006-2928
• DOI: 10.1007/bf00485798

✦ Synopsis

Limulus polyphemus has two electrophoretically distinct arginine kinases, a negative and a neutral (at pH 8.6). The highest concentrations of the neutral are found in muscle, where the total arginine kinase activity is highest. The peptide maps of the two forms are very similar, but the negative has six more acidic peptides than the neutral. Three tryptophan-containing peptides were isolated from tryptie digests of each form. The amino acid compositions of two of the three pairs of peptides were different. This sugests that the isoenzymes are the products of two distinct genes.