Further characterization of turkey trypsin: End groups and sequence of histidine-containing peptides

Kishida, Tadaaki; Liener, Irvin E.

doi:10.1016/0003-9861(68)90565-1

Cited by 9 publications

(4 citation statements)

References 36 publications

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“…Abbreviations: RCT, rat cationic trypsinogen; AN1, rat anionic trypsinogen I; AN2, rat anionic trypsinogen II; PCT, porcine cationic trypsin; ST, sheep trypsinogen; HT1, human trypsinogen I; HT2, human trypsinogen II; TT, turkey trypsinogen; BCT, bovine cationic trypsinogen; HCT, human cationic trypsinogen. Sequences are from the following: AN1 and AN2, Craik et al (1984); PCT, Hermodson et al (1973); ST, Dayhoff (1969); HT1 and HT2, Guy et al (1978); TT, Kishida & Liener (1968); BCT, Hartley (1970); and HCT, Brodrick et al (1978). figure 4: Net cumulative charge of rat cationic trypsin (dotted line) and rat anionic trypsin I (solid line).…”

Section: Resultsmentioning

confidence: 99%

Isolation and characterization of a cDNA encoding rat cationic trypsinogen

Fletcher¹,

Alhadeff²,

Craik³

et al. 1987

Biochemistry

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A cDNA encoding rat cationic trypsinogen has been isolated by immunoscreening from a rat pancreas cDNA library. The protein encoded by this cDNA is highly basic and contains all of the structural features observed in trypsinogens. The amino acid sequence of rat cationic trypsinogen is 75% and 77% homologous to the two anionic rat trypsinogens. The homology of rat cationic trypsinogen to these anionic trypsinogens is lower than its homology to other mammalian cationic trypsinogens, suggesting that anionic and cationic trypsins probably diverged prior to the divergence of rodents and ungulates. The most unusual feature of this trypsinogen is the presence of an activation peptide containing five aspartic acid residues, in contrast to all other reported trypsinogen activation peptides which contain four acidic amino acid residues. Comparisons of cationic and anionic trypsins reveal that the majority of the charge changes occur in the C-terminal portion of the protein, which forms the substrate binding site. Several regions of conserved charge differences between cationic and anionic trypsins have been identified in this region, which may influence the rate of hydrolysis of protein substrates.

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Section: Resultsmentioning

confidence: 99%

Isolation and characterization of a cDNA encoding rat cationic trypsinogen

Fletcher¹,

Alhadeff²,

Craik³

et al. 1987

Biochemistry

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“…Less purified samples of chicken trypsin and turkey chymotrypsin have also been obtained (Ryan, 1965). Kishida and Liener (1968) made a further study of crystalline turkey trypsin with respect to the sequence of amino acids and end groups. Chicken chymotrypsin (MW 20,000) exhibited esterase activity almost twice that of bovine a-chymotrypsin but only two thirds of the protease activity .…”

Section: Digestion In the Small Intestinementioning

confidence: 99%

Avian Physiology

1976

Springer Advanced Texts in Life Sciences

140

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“…Trypsin has been isolated from the pancreas of a number of animal sources including bovine [3], porcine [4,5], ovine [5,6], goat [7], moose [8], whale [9], elephant seal [10], African lungfish [11], swine [12,13], rat [14], turkey [15,16] and human [17,18]. Comparative studies reported by several workers [4][5][6]15,16,19] suggest that mammalian trypsins are very similar in their gross physical and chemical properties but may differ significantly in amino acid composition.…”

Section: Introductionmentioning

confidence: 99%

“…Comparative studies reported by several workers [4][5][6]15,16,19] suggest that mammalian trypsins are very similar in their gross physical and chemical properties but may differ significantly in amino acid composition. Sinha and Das [20] reported the isolation of trypsin from goat pancreatic extract and its crystallization.…”

Section: Introductionmentioning

confidence: 99%