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• W2078687600 abstract "Proteins BASP1 and GAP-43/B-50, which are abundant in nerve endings, show a number of similar physico-chemical properties. Nevertheless, they belong to different protein families. In this work, complete amino acid sequences of bovine BASP1 and human BASP1 were established. They proved to be very similar to the sequences of rat brain protein NAP-22 and chicken brain protein CAP-23. Relatively to human BASP1 its bovine, rat and chicken analogues show 80%, 70% and 45% sequence identity respectively, confirming their membership of a definite protein family (BASP1 family). All members of BASP1 family contain several 'good' PEST sequences characteristic for short-living proteins. Conservation of PEST sequences in BASP1 of different species points to their significance for BASP1 functions. In contrast to GAP-43/B-50 showing high immunological cross-reactivity between the proteins belonging to different species of mammals, immunological properties of BASP1 are species specific. BASP1 shows both high hydrophilicity and some properties characteristic for hydrophobic proteins. These properties are caused by N-terminal myristoylation of BASP1 molecules. Unlike GAP-43/B-50, BASP1 is present in high amounts also in some non-nervous tissues: testis, kidney and lymphoid organs (spleen, thymus). So far examined characteristics, including myristoylation, peptide maps and detected by isoelectrofocusing microheterogeneity, proved to be the same for BASP1 samples isolated from both brain and non-nervous tissues. Therefore, in spite of different physiological consequences, biochemical functions of BASP1 must also be similar in different tissues." @default.
• W2078687600 created "2016-06-24" @default.
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• W2078687600 date "1997-06-01" @default.
• W2078687600 modified "2023-09-27" @default.
• W2078687600 title "The BASP1 family of myristoylated proteins abundant in axonal termini. Primary structure analysis and physico-chemical properties" @default.
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• W2078687600 doi "https://doi.org/10.1016/s0300-9084(97)80032-6" @default.
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