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F Bossa

Publications and source records attributed to F Bossa.

At least 145 records · Page 8Linked to original sources
PubMed1973

The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with thermolysin and elastase.

Peptides produced by thermolytic digestion of aminoethylated aspartate aminotransferase and of the oxidized enzyme were isolated and their amino acid sequences determined. Digestion by elastase of the carboxymethylated enzyme gave peptides representing approximately 40% of the primary structure. Fragments from these digests overlapped with previously reported sequences of peptides obtained by peptic and tryptic digestion (Doonan et al., 1972), giving ten composite peptides containing 395 amino acid residues. The amino acid composition of these composite peptides agrees well with that of the intact enzyme. Confirmatory results for some of the present data have been deposited as Supplementary Publication 50018 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973) 131, 5.

Amino Acid Sequence↗
PubMed1972

The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with pepsin and trypsi trypsin.

Peptides obtained by tryptic digestion of carboxymethylated and maleylated aspartate aminotransferase and of the aminoethylated enzyme were isolated and the complete amino acid sequences of most of them were determined. Digestion of the carboxymethylated protein with pepsin produced a complex mixture of peptides that allowed some overlapping of the tryptic peptides (Fig. 4); in addition, peptides were obtained that had not been found in either of the tryptic digests. From these studies about 400 amino acid residues were identified. Experimental details and confirmatory data for the results presented here are given in a supplementary paper that has been deposited as Supplementary Publication 50011 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1972) 126, 5.

Alkylation↗
PubMedDate not supplied

Six novel tachykinin- and bombesin-related peptides from the skin of the Australian frog Pseudophryne güntheri.

Six novel peptides belonging to the tachykinin and bombesin families were isolated and sequenced from extracts of the skin of the Australian myobatrachid frog Pseudophryne güntheri. One of these peptides (PG-L) was of the bombesin family and may be considered an N-elongation of the litorin/ranatensin molecule, with which it shares an identical spectrum of activity on isolated smooth muscle preparations. The other five peptides were of the tachykinin family with two of these peptides (PG-SPI and PG-SPII) related to substance P and three (PG-KI, PG-KII and PG-KIII) to kassinin. In contrast to the basic nature of substance P, the PG-SP peptides showed a clear acidic character and displayed a more potent and sustained action on isolated smooth muscle preparations and rat blood pressure than did substance P. Two of the three PG-K peptides were more potent than kassinin; PG-KIII was considerably less potent. PG-KI and PG-KII were also present in a deamidated, poorly active, form.

Amino Acid Sequence↗