scholarly journals CATABOLIC ORIGIN OF A BENCE JONES PROTEIN FRAGMENT

1968 ◽  
Vol 128 (3) ◽  
pp. 517-532 ◽  
Author(s):  
D. Cioli ◽  
C. Baglioni
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Peptide Mapping ◽  
Gel Filtration ◽  
Urinary Proteins ◽  
Small Peptides ◽  
Protein Fragment ◽  
Bence Jones Protein ◽  
Bence Jones Proteins

Gel filtration analysis of the urinary proteins of some patients with myeloma has shown the presence of "fragments" of Bence Jones proteins which correspond to the variable half of these proteins. Experiments have been carried out to establish the origin of a "fragment" observed in a patient who excreted a large amount of this protein. Labeled homologous Bence Jones protein has been injected into this and other control patients. Excretion of labeled "fragment" has been observed in all. Analysis by peptide mapping and radio-autography of this labeled "fragment" isolated from the urine showed that the invariable half of the Bence Jones protein was not excreted; it seemed thus likely that the invariable half was metabolized to small peptides and free amino acids. A labeled Bence Jones protein which was excreted without any accompanying "fragment" was injected into the patient who excreted large amounts of "fragment." No excretion of labeled "fragment" was observed. It was thus concluded that the property of being degraded to "fragment" is characteristic of some "fragile" Bence Jones proteins and is not determined by the patient. Incubation with serum or urine of the "fragile" Bence Jones protein failed to produce any "fragment." "Fragments" of Bence Jones proteins are thus most likely formed during excretion of these proteins through the kidney and are products of the catabolism of Bence Jones proteins.

Contribution of rennet and starter proteases to proteolysis in Cheddar cheese

1976 ◽  
Vol 43 (1) ◽  
pp. 97-107 ◽  
Author(s):  
R. B. O'Keeffe ◽  
P. F. Fox ◽  
C. Daly
Keyword(s):  
Amino Acids ◽  
Gel Electrophoresis ◽  
Free Amino Acids ◽  
Free Amino ◽  
Gel Filtration ◽  
Cheddar Cheese ◽  
Limited Range ◽  
Peptidase Activity ◽  
Small Peptides ◽  
Micro Organisms

SummaryProteolysis in aseptic, chemically acidified (GDL) cheese and in starter cheese made under controlled bacteriological conditions (i.e. free of non-starter micro-organisms) was measured by gel electrophoresis, the formation of pH 4·6- and 12% TCA-soluble N, gel filtration and the liberation of free amino acids. The results show that rennet was mainly responsible for the level of proteolysis detected by gel electrophoresis, pH 4·6-soluble N and gel filtration i.e. large, medium and small peptides. However, rennet alone was capable of producing only a limited range of free amino acids; only methionine, histidine, glycine, serine and glutamic acid were produced at quantifiable levels (> 0·2 μmoles/g) in GDL cheese; it is suggested that free amino acids in Cheddar cheese are mainly the result of microbial peptidase activity. The levels of free amino acids in the starter cheese were considerably lower than values reported for commercial Cheddar.

Proteolysis in Cheddar cheese: role of coagulant and starter bacteria

1978 ◽  
Vol 45 (3) ◽  
pp. 465-477 ◽  
Author(s):  
Arthur M. O'Keeffe ◽  
Patrick F. Fox ◽  
Charles Daly
Keyword(s):  
Amino Acids ◽  
High Voltage ◽  
Free Amino Acids ◽  
Free Amino ◽  
Protein Solubility ◽  
Gel Filtration ◽  
Cheddar Cheese ◽  
Paper Electrophoresis ◽  
Small Peptides

SummaryCheddar cheese was produced free of non-starter bacteria, acidified with starter or glucono-δ-lactone and containing active coagulant (chymosin or pepsin) or inactivated coagulant (pepsin). The level and type of proteolysis in the experimental cheeses was monitored by protein solubility at pH 4·6 and in 12 % TCA, polyacrylamide gel and high voltage paper electrophoresis, gel filtration and paper chromatography. The results show that the coagulant was primarily responsible for the formation of large peptides while small peptides and free amino acids were produced principally by the starter, possibly from coagulant-produced peptides.

EXTRACELLULAR ORGANIC NITROGEN IN USTILAGO MAYDIS FERMENTATION BROTHS

1956 ◽  
Vol 34 (1) ◽  
pp. 1195-1198
Author(s):  
Eugene L. Dulaney ◽  
E. Bilinski ◽  
W. B. McConnell
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Organic Nitrogen ◽  
Ustilago Maydis ◽  
Ammonia Nitrogen ◽  
Small Peptides ◽  
Lysine Concentration ◽  
High Level ◽  
Fermentation Broths

Free amino acids and small peptides make up most of the extracellular organic nitrogen in media from shaken and aerated Ustilago maydis fermentations. Of the 3.5 mgm./ml. ammonia nitrogen added, 2.9 mgm./ml. remained in the extracellular broth. This extracellular nitrogen contained 1.17 mgm./ml. of organic nitrogen and 1.74 mgm./ml. of residual ammonia nitrogen. At least 53% of extracellular organic nitrogen is in the form of free amino acids. Fifteen amino acids were estimated quantitatively in acid-hydrolyzed broth and a particularly high level of arginine (1.14 mgm./ml.) was found. The amounts of methionine and tryptophan in the broth were quite low but the lysine concentration 0.400 mgm./ml. was relatively high.

Analytische Untersuchungen des Wehrsekretes von Peripatopsis moseleyi (Onychophora) / Analytical Investigations of the Defensive Secretion from Peripatopsis moseleyi (Onychophora)

1977 ◽  
Vol 32 (1-2) ◽  
pp. 57-b ◽  
Author(s):  
Harald Röper
Keyword(s):  
Amino Acids ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Defensive Secretion ◽  
Gel Filtration ◽  
Total Content ◽  
Gas Liquid Chromatography ◽  
Isoleucine Leucine

The defensive secretion of Peripatopsis moseleyi (Onychophora) consists of 84% water and 16% protein and free amino acids. The secretion’s defensive effectiveness is an anti-predator “sticking” action. The secretion is flung out of the oral papillae in liquid state. It is then denaturized by the air and develops increasingly sticky white threads, probably through the devel­opment of disulfide bridges from the protein content. The elastic properties of the secretion threads indicate a micellar structure. The defensive secretion contains no volatile organic components or carbohydrates. This was confirmed by gas- liquid chromatography and thin-layer chromatography. After acidic hydrolysis of the secretion the following amino acids were determined quantita­tively: aspartic acid, threonine, serine, proline, glutamic acid, glycine, alanine, valine, cysteine, methionine, isoleucine, leucine, tyrosine, phenylalanine, lysine, histidine and arginine. A “rare” amino acid was not identified. Tryptophane was not present (basic secretion hydrolysis). The quantita­tive determination of free amino acids, based on the total content, showed the following results: glycine (40.9%), glutamic acid (10.8%), aspartic acid (2.65%), lysine (1.3%). This result shows, that the secretion is stored in a watery glycine/glutaminic acid buffer in the oral papillae of Peripatopsis moseleyi. High voltage paper electrophoreses and gel filtration experiments with dextran and agarose gels showed, that the secretion protein consists of, at least, two fractions with different molecular weight.

The venom of the honeybee (Apis mellifera): free amino acids and peptides

1968 ◽  
Vol 46 (10) ◽  
pp. 1221-1226 ◽  
Author(s):  
David A. Nelson ◽  
Rod O'Connor
Keyword(s):  
Amino Acids ◽  
Apis Mellifera ◽  
Amino Acid ◽  
Solvent Extraction ◽  
Free Amino Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Gel Filtration ◽  
Automated Analysis ◽  
Electrical Excitation

The venom of the honeybee (Apis mellifera), obtained by electrical excitation, was fractionated by solvent extraction and gel filtration. The free amino acid and peptide content was determined by automated analysis. Less than 1% of the venom consisted of 19 free amino acids, while the minimum quantity of the 14 peptides was 15%. Two histapeptides were isolated and characterized. The sequence of histapeptide A was alanyl-glycyl-prolyl-alanyl-glutaminyl-histamine.

EXTRACELLULAR ORGANIC NITROGEN IN USTILAGO MAYDIS FERMENTATION BROTHS

1956 ◽  
Vol 34 (6) ◽  
pp. 1195-1198 ◽  
Author(s):  
Eugene L. Dulaney ◽  
E. Bilinski ◽  
W. B. McConnell
Keyword(s):  
Amino Acids ◽  
Free Amino Acids ◽  
Free Amino ◽  
Organic Nitrogen ◽  
Ustilago Maydis ◽  
Ammonia Nitrogen ◽  
Small Peptides ◽  
Lysine Concentration ◽  
High Level ◽  
Fermentation Broths

Free amino acids and small peptides make up most of the extracellular organic nitrogen in media from shaken and aerated Ustilago maydis fermentations. Of the 3.5 mgm./ml. ammonia nitrogen added, 2.9 mgm./ml. remained in the extracellular broth. This extracellular nitrogen contained 1.17 mgm./ml. of organic nitrogen and 1.74 mgm./ml. of residual ammonia nitrogen. At least 53% of extracellular organic nitrogen is in the form of free amino acids. Fifteen amino acids were estimated quantitatively in acid-hydrolyzed broth and a particularly high level of arginine (1.14 mgm./ml.) was found. The amounts of methionine and tryptophan in the broth were quite low but the lysine concentration 0.400 mgm./ml. was relatively high.

Changes in Free Amino Acids in Skeletal Muscle of Cod (Gadus morhua) Under Conditions Simulating Gillnet Fishing

1968 ◽  
Vol 25 (5) ◽  
pp. 935-942 ◽  
Author(s):  
N. Dambergs ◽  
P. Odense ◽  
R. Guilbault
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Amino Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Gadus Morhua ◽  
Small Peptides ◽  
Free Amino Acid Pool ◽  
Amino Acid Analyser ◽  
Muscular Tissues

The total amounts of free amino acids, comprising both the intracellular and plasmal pools, as well as the amino acids combined in small peptides were determined with an automatic amino acid analyser in muscular tissues of freshly killed cod and in cod suffocated in simulated gillnetting conditions. The total amount of the free amino acids in the musculature was 2.4% of the amino acids composing the proteins. More than 90% of the free amino acid pool was represented by histidine, taurine, glycine, alanine, lysine, and β-alanine. The amino acids that were not found in small peptides are taurine, alanine, threonine, lysine, tyrosine, cystine, and methionine. In the absence of flexion or handling of the suffocated fish there was no evidence of enzymatic processes up to 72 hr after death. There was a slight, continuous loss of the free amino acids from the intact body of the fish during the prerigor and rigor periods. No evidence of deaminase activity affecting the amino acids was detected. Histidine, with its methyl homologues, was the major free amino acid.

scholarly journals A STUDY OF IMMUNOGLOBULIN STRUCTURE

1969 ◽  
Vol 130 (2) ◽  
pp. 401-415 ◽  
Author(s):  
R. Quattrocchi ◽  
D. Cioli ◽  
C. Baglioni
Keyword(s):  
Light Chain ◽  
Peptide Mapping ◽  
Gel Filtration ◽  
Antigenic Determinants ◽  
Minimal Size ◽  
Bence Jones Protein ◽  
Peptide Map ◽  
Peptide Maps ◽  
Similar Peptide ◽  
Bence Jones Proteins

102 human Bence Jones proteins have been purified by gel filtration, digested with trypsin, and analyzed by peptide mapping. In several cases Bence Jones "fragments", corresponding to the variable half of the corresponding proteins, were observed. The peptide maps of the proteins were compared to establish whether any identical proteins were present in the sample analyzed. No Bence Jones protein showed a peptide map identical to that of any other protein, although remarkable similarities in the peptide maps were observed for some proteins. Two proteins that gave very similar peptide maps were then examined in detail, by purifying and analyzing the tryptic peptides. It was then found that these two proteins differ in amino acid sequence in at least six positions. The probability of not finding two identical sequences by examining a sample extracted from populations of light chains of different sizes has been calculated. This has led to an estimate of the minimal size of the population of light chain sequences in humans. The number of light chain sequences appears to be at least a few thousand. Information on the frequency of Inv and Oz antigenic determinants and on the relative frequency of subtypes of K chains has been obtained. Proteins of KI subtype are found most frequently. The possibility that different subtypes may be predominant in different species is discussed in relation to the evolutionary arguments used in favor of the somatic theories on the origin of variability of immunoglobulin chains.

scholarly journals A STUDY OF IMMUNOGLOBULIN STRUCTURE

1966 ◽  
Vol 124 (3) ◽  
pp. 307-330 ◽  
Author(s):  
C. Baglioni ◽  
D. Cioli
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Peptide Mapping ◽  
Gel Filtration ◽  
Bence Jones Protein ◽  
Type K ◽  
The Common ◽  
L Proteins ◽  
Peptide Maps ◽  
Bence Jones Proteins

Urinary proteins of patients with myeloma, prepared by precipitation with ammonium sulphate, have been separated by gel filtration on Sephadex G-100 after reduction and aminoethylation. Many specimens separated into a major peak of Bence Jones protein and into minor peaks of albumin, a protein tentatively identified with heavy chain and a smaller molecular weight protein corresponding to the variable portion of the corresponding Bence Jones protein. The Bence Jones protein purified by gel filtration was analyzed by electrophoresis and by peptide mapping after tryptic digestion. The peptide maps of 24 type K and 20 type L Bence Jones proteins were compared. A set of common peptides was identified in the peptide maps of the Bence Jones proteins of the same type; the common peptides of type K proteins were completely different from the common peptides of type L proteins. The patterns of distinctive peptides was compared; no similarities were found between distinctive peptides of type K and of type L proteins. Some similarities were observed in the distinctive peptides of proteins of the same type. The similarities involved in many cases peptides containing cysteine, whereas similarities in other peptides were limited. This observation suggested that the amino acid sequence around the cysteines of the variable NH2-terminal half of the Bence Jones proteins may show less variability than other sequences. A few proteins of the same type differed in all their distinctive peptides, an indication that multiple amino acid differences exist between individual Bence Jones proteins. The genetic mechanisms responsible for the variability in the amino acid sequence of the NH2-terminal half of the light chains of immunoglobulins are discussed in view of the results of the comparison by peptide mapping of the Bence Jones proteins.

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