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- W2003994723 abstract "Plasma samples from two members of the Salmonidae family, the chinook salmon (Oncorhynchus tshawytscha) and brown trout (Salmo trutta), were examined. Albumin, initially identified as the predominant anionic palmitate-binding band on agarose gel electrophoresis of plasma, was purified from both species by DEAE-ion exchange chromatography. Albumin has a plasma concentration of approximately 15 mg/ml in both species. Like other fish species, neither trout nor salmon albumin binds nickel; a characteristic of many mammalian albumins. Salmon and trout albumins have molecular masses of 65 and 67 kDa, respectively, indicating some sequence differences. However, N-terminal sequencing of the first 15 residues of both these proteins indicated identical sequences of 1QNQICTIFTEAKEDG15-. This showed that the mature N-terminal sequence (SQAQNQICTIFTEAKEDG-) predicted from the cDNA of Atlantic salmon albumin is in fact incorrect, with the actual N-terminus for salmonids starting three amino acids later than that predicted. Examination of the Atlantic salmon cDNA sequence suggested that salmonid albumin is unique, in lacking a propeptide. No proalbumin convertase site (RXYR/XYRR) is present and it appears that the salmonid albumin precursor is cleaved only by the signal peptidase, between -1 Ala and +1 Gln, to produce mature albumin. This site has a preferrred motif for the signal peptidase of -1 Ala and -3 Ser, as well as -2 Gln. Thus, salmonid albumin possesses a 21-residue prepeptide, but no propeptide." @default.
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- W2003994723 date "1998-02-01" @default.
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- W2003994723 title "The Albumins of Chinook Salmon (Oncorhynchus tshawytscha) and Brown Trout (Salmo trutta) Appear to Lack a Propeptide" @default.
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- W2003994723 doi "https://doi.org/10.1006/abbi.1997.0509" @default.
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