Title : Synthesis and pharmacology of nonmammalian angiotensins and their evolutionary development.

Pub. Date : 1985

PMID : 3841691






3 Functional Relationships(s)
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Protein Name
Organism
1 These studies indicated the presence of a new L-asparaginase amidohydrolase type enzyme in eel plasma which deamidates L-asparagine residue at the amino terminus of the angiotensin peptides, thereby implying that l-asparaginyl decapeptide (rather than l-aspartyl decapeptide) is the natural form of angiotensin inherent in eel plasma. Asparagine asparaginase and isoaspartyl peptidase 1 Homo sapiens
2 These studies indicated the presence of a new L-asparaginase amidohydrolase type enzyme in eel plasma which deamidates L-asparagine residue at the amino terminus of the angiotensin peptides, thereby implying that l-asparaginyl decapeptide (rather than l-aspartyl decapeptide) is the natural form of angiotensin inherent in eel plasma. l-asparaginyl decapeptide asparaginase and isoaspartyl peptidase 1 Homo sapiens
3 These studies indicated the presence of a new L-asparaginase amidohydrolase type enzyme in eel plasma which deamidates L-asparagine residue at the amino terminus of the angiotensin peptides, thereby implying that l-asparaginyl decapeptide (rather than l-aspartyl decapeptide) is the natural form of angiotensin inherent in eel plasma. l-aspartyl decapeptide asparaginase and isoaspartyl peptidase 1 Homo sapiens