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V B Pedersen

Publications and source records attributed to V B Pedersen.

6 recordsLinked to original sources
PubMed1979

The primary structure of calf chymosin.

The complete amino acid sequence of calf chymosin (rennin) (EC 3.4.23.4) has been determined. The sequence consists of a single peptide chain of 323 amino acid residues. The primary structure of the precursor part of calf prochymosin was published previously (Pedersen, V.B., and Foltmann, B. (1975) Eur. J. Biochem. 55, 95-103), thus we are now able to account for the total 365 amino acid residues of calf prochymosin. Comparison of the sequence of calf prochymosin with that of pig pepsinogen A (EC 3.4.23.1) shows extensive homology. In the precursor part of the sequence, 15 residues are located at identical positions, as compared to 189 identical residues in the respective enzymes. Furthermore comparison to Penicillium janthinellum acid proteinase (penicillopepsin) (EC 3.4.23.7) shows that 76 residues are common to this enzyme and to the two gastric proteinases. These homologies in sequence further suggest that the folding of the peptide chain in chymosin is very similar to that of other acid proteinases.

Amino Acid Sequence↗
PubMed1979

Investigations on the activation of bovine prochymosin.

Activation of prochymosin at pH below 2.5 results in formation of the active enzyme pseudochymosin by proteolytic cleavage of the bond 27--28. Pseudochymosin is 15 amino acid residues longer than chymosin. It is the final activation product at low pH, whereas chymosin is formed by activation between pH 4 and 5. Pseudochymosin is converted to chymosin when it is brought to pH 5.5. Our present knowledge does not allow quantitative evaluation of the possible reactions involved in formation of pseudochymosin, but the course of activation at pH 2 is in accordance with an intermolecular reaction between two zymogen molecules as the predominant reaction. We find indications of an intramolecular reaction when intermolecular reactions are prevented by immobilization of the zymogen.

Amino Acid Sequence↗
PubMed1977

Comparison of the primary structures of acidic proteinases and of their zymogens.

From the scattered information about primary structures of aspartate proteinases the following general features appear: 1) Sequence determinations show that two catalytically active aspartic acid residues are located in highly conservative surroundings. 2) Zymogens have so far only been found for extracellular aspartate proteinases of the vertebrates. The zymogens from the gastric mucosa are converted into active enzymes by a limited proteolysis releasing 42 to 44 residues from the NH2-terminus. A common pattern of basic and apolar residues is observed in this NH2-terminal segment. 3) In the presently known structures gastric proteinases and their zymogens have about 40% of all residues in common. The sequence of penicillopepsin shows 18% of identity with the gastric proteinases.

Amino Acid Sequence↗
PubMed1977

The complete amino acid sequence of prochymosin.

The total sequence of 365 amino acid residues in bovine prochymosin is presented. Alignment with the amino acid sequence of porcine pepsinogen shows that 204 amino acid residues are common to the two zymogens. Further comparison and alignment with the amino acid sequence of penicillopepsin shows that 66 residues are located at identical positions in all three proteases. The three enzymes belong to a large group of proteases with two aspartate residues in the active center. This group forms a family derived from one common ancestor.

Amino Acid Sequence↗
PubMed1975

Amino-acid sequence of the peptide segment liberated during activation of prochymosin (prorennin).

By conversion of prochymosin into active chymosin and N-terminal segment of 42 amino acid residues is liberated. In one activation experiment this segment was recovered in two peptides; in a second experiment the activation segment was cleaved into three peptides. The primary structures of the peptides have been determined. Overlaps between these peptides and between the activation segment and the active enzyme have been obtained from peptides produced by tryptic digestion of denatured prochymosin. Comparison of the amino acid sequences of the activation segments from bovine prochymosin, bovine pepsinogen and porcine pepsinogen shows considerable homology.

Amino Acid Sequence↗