The Porcine Pancreatic Carboxypeptidase A System

Folk, J.E.; Schirmer, Eva

doi:10.1016/s0021-9258(18)51803-2

Cited by 339 publications

(28 citation statements)

References 14 publications

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“…0306-3275/82/080449-04$01.50/1 ©) 1982 The Biochemical Society Both proenzymes were treated with 1 mM-phenylmethanesulphonyl fluoride before being stored in the form of a precipitate, in (NH4)2SO4, at 40C. Carboxypeptidase A (EC 3.4.17.1) activities were measured against the substrate N-benzoylglycyl-Lphenylalanine at 1 mm concentration (Folk & Schirmer, 1963). Proteinase E activities were measured against N-succinyl-L-alanylalanylalanine pnitroanilide at 1 mm concentration (Bieth et al, 1974).…”

Section: Methodsmentioning

confidence: 99%

Isolation and re-association of the subunits from the pro-(carboxypeptidase A)–pro-(proteinase E) binary complex from pig pancreas

Vendrell

Avilés

Segundo

et al. 1982

Biochemical Journal

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The component subunits of the pro-(carboxypeptidase A)-pro-(proteinase E) binary complex from pig pancreas were separated with a high recovery (80-95%) of their original potential activity. The isolated subunits and the reconstituted complex have properties similar to those of the corresponding natural species. The tryptic activation course of the pro-(carboxypeptidase A) subunit is substantially modified when bound to pro-(proteinase E), whereas the activation of pro-(proteinase E) is not dependent on this association.

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Section: Methodsmentioning

confidence: 99%

Isolation and re-association of the subunits from the pro-(carboxypeptidase A)–pro-(proteinase E) binary complex from pig pancreas

Vendrell

Avilés

Segundo

et al. 1982

Biochemical Journal

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“…Pepsin, with a stated activity of 2530 units/mg (lot no. PM9FD), DFP-treated carboxypeptidase A with a measured activity of 45 units/mg (assayed using hippuryl-L-phenylalanine as described by Folk and Schirmer, 1963), and yeast RNA (type XI, lot no. 98B-8050) were Worthington products.…”

Section: Methodsmentioning

confidence: 99%

Conformation and conformational stability of ribonuclease A and its peptic derivative, des-(121-124)-ribonuclease

Puett¹,

Wasserman²,

Friebele³

1972

Biochemistry

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We have determined the near-ultraviolet circular dichroic spectrum (235-315 nm) and the ultraviolet difference absorption spectrum of ribonuclease A (RNase A) and its peptic derivative, des-(121-124)-RNase A (RNase P), which is missing the four C-terminal residues and retains no more than a few per cent of the enzymic activity of RNase A. The circular dichroic spectra of both proteins were resolved into gaussian parameters and the rotational strengths of the resolved bands (due mainly to tyrosines and disulfides) were found to be very similar in the two proteins. Also, the denaturation difference spectrum was almost identical, thus indicating that in each native protein the same number of tyrosyl groups are inaccessible to solvent. The circular dichroic spectrum of RNase P between 195 and 235 nm was also obtained and compared to the known spectrum of RNase A. The gen-

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“…The total soluble protein was determined as per Lowry et al (1951) in a UV-VIS spectrophotometer (UV-1800, Shimadzu, Japan). All the digestive enzymes, including pepsin, trypsin, chymotrypsin, amylase, carboxypeptidase-A, carboxypeptidase-B, acid phosphatase, alkaline phosphatase and lipase were measured as per the methods described by Anson (1938), Erlanger et al (1961), Hummel (1959), Bernfeld (1955), Folk and Schirmer (1963), Folk et al (1960), Walter and Schutt (1974) and Winkler and Stuckmann (1979) respectively and their activity was expressed as U mg protein -1 .…”

Section: Biochemical Analysismentioning

confidence: 99%

A blend of plant proteins as a potential fishmeal substitute in the diet of Asian seabass Lates calcarifer (Bloch-1790): Effect on growth, digestive enzymes and fatty acid composition

Madhubabu¹,

Jannathulla²,

Khan³

et al. 2021

Indian Journal of Fisheries

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A blend of plant proteins (soybean meal, groundnut oil cake, sunflower oil cake, wheat gluten meal and corn gluten meal at 4:2:1:6.5:6.5) was used to substitute fishmeal in the diet of Asian seabass Lates calcarifer (Bloch, 1790). Five iso-nitrogenous (401.13-407.33 g kg -1 ) diets were prepared by substituting fishmeal at 0 (control), 25, 50, 75 and 100% (FM-R0, FM-R25, FM-R50, FM-R75 and FM-R100, respectively) using the above mix. Average final weight of the fish increased (p<0.05) by three-folds (20.77-29.99 g) after 45 days compared to their initial weight (6.09±0.25 g) in all the treatments, however, significant (p<0.05) variation was observed between the dietary treatments (p<0.002). The results indicated that 50% of dietary fishmeal can be substituted and beyond this level resulted in significant reduction of growth performance. Broken-line analysis indicated optimal fishmeal substitution as 46.7%. The highest activity of pepsin, trypsin, chymotrypsin, carboxypeptidases-A and B was observed in fish fed with diets FM-R0, FM-R25 and FM-R50. Dietary change significantly (p<0.05) influenced the carcass lipid composition of Asian seabass (p<0.001). Fatty acids like C20:4, C20:5 and C22:6 were significantly (p<0.05) low in fish carcass fed with higher levels of plant proteins (FM-R75 and FM-R100). The results concluded that dietary fishmeal level can be partially substituted using a blend of plant proteins in the diet of Asian seabass juveniles.

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The Porcine Pancreatic Carboxypeptidase A System

Cited by 339 publications

References 14 publications

Isolation and re-association of the subunits from the pro-(carboxypeptidase A)–pro-(proteinase E) binary complex from pig pancreas

Isolation and re-association of the subunits from the pro-(carboxypeptidase A)–pro-(proteinase E) binary complex from pig pancreas

Conformation and conformational stability of ribonuclease A and its peptic derivative, des-(121-124)-ribonuclease

A blend of plant proteins as a potential fishmeal substitute in the diet of Asian seabass Lates calcarifer (Bloch-1790): Effect on growth, digestive enzymes and fatty acid composition

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