scholarly journals The protein–polysaccharide complex of bovine nasal cartilage. Studies on the protein core

1967 ◽  
Vol 105 (2) ◽  
pp. 569-575 ◽  
Author(s):  
A Serafini-Fracassini ◽  
T. J. Peters ◽  
L. Floreani
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Protein Content ◽  
Amino Acid Analysis ◽  
Cetylpyridinium Chloride ◽  
Amino Acid Compositions ◽  
Nasal Cartilage ◽  
Polysaccharide Complex ◽  
End Group

1. Chondromucoprotein from bovine nasal cartilage was purified by cetylpyridinium chloride or by bismuth nitrate in acetone. 2. Amino acid compositions of crude and purified preparations were compared and few differences were found, in spite of the decrease in protein content on purification. 3. Amino acid analysis of bismuth-purified material revealed the existence of four groups of amino acids. Within each group, the amino acids were present in approximately equimolar concentrations. 4. Amino end-group assay on the same material showed six α-DNP derivatives. 5. A molecular weight of 6·3×105 for the protein–polysaccharide complex was calculated from the latter analysis.

scholarly journals Amino Acid Compositions of 27 Food Fishes and Their Importance in Clinical Nutrition

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Bimal Mohanty ◽  
Arabinda Mahanty ◽  
Satabdi Ganguly ◽  
T. V. Sankar ◽  
Kajal Chakraborty ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Content ◽  
High Performance ◽  
Crude Protein ◽  
Cold Water ◽  
Building Blocks ◽  
Crude Protein Content ◽  
Dietary Counseling ◽  
Amino Acid Compositions

Proteins and amino acids are important biomolecules which regulate key metabolic pathways and serve as precursors for synthesis of biologically important substances; moreover, amino acids are building blocks of proteins. Fish is an important dietary source of quality animal proteins and amino acids and play important role in human nutrition. In the present investigation, crude protein content and amino acid compositions of important food fishes from different habitats have been studied. Crude protein content was determined by Kjeldahl method and amino acid composition was analyzed by high performance liquid chromatography and information on 27 food fishes was generated. The analysis showed that the cold water species are rich in lysine and aspartic acid, marine fishes in leucine, small indigenous fishes in histidine, and the carps and catfishes in glutamic acid and glycine. The enriched nutrition knowledge base would enhance the utility of fish as a source of quality animal proteins and amino acids and aid in their inclusion in dietary counseling and patient guidance for specific nutritional needs.

scholarly journals DETERMINATION OF CERTAIN AMINO ACIDS IN CHYMOTRYPSINOGEN, AND ITS MOLECULAR WEIGHT

1941 ◽  
Vol 25 (2) ◽  
pp. 167-176 ◽  
Author(s):  
Erwin Brand ◽  
Beatrice Kassell
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Osmotic Pressure ◽  
Amino Acid Analysis ◽  
Pressure Measurements ◽  
Sulfur Amino Acids ◽  
Sh Groups

1. A preparation of chymotrypsinogen, obtained from Dr. M. Kunitz, was analyzed for sulfur, the sulfur amino acids, tyrosine, and tryptophane. 2. The protein sulfur of chymotrypsinogen was accounted for as methionine, cysteine, and cystine. 3. A method is presented for calculating the minimum molecular weight of a protein from the distribution of the sulfur amino acids. In the case of chymotrypsinogen, the calculated minimum molecular weight was found to be the actual molecular weight. 4. The molecular weight of chymotrypsinogen is 36,700 by amino acid analysis as compared to 36,000 by osmotic pressure measurements of Kunitz and Northrop. Chymotrypsinogen contains per mol 17 atoms of sulfur, 3 residues of methionine, 4 of cysteine, 10 of half-cystine (i.e. 5 S—S linkages), 6 of tyrosine, and 10 of tryptophane. 5. The tryptophane content of chymotrypsinogen (5.51 per cent) is the highest of any protein so far on record. 6. Chymotrypsinogen contains no reactive SH groups, although it yields cysteine on hydrolysis. This may be due either to preformed but unreactive SH groups or to S—X groups. The term S—X group is used to denote the substitution of the sulfhydryl hydrogen by a constituent X; hydrolysis yields SH groups: S—X + HOH = SH + X—OH.

Complete Covalent Structure of Human Platelet Factor 4

1979 ◽  
Vol 42 (05) ◽  
pp. 1652-1660 ◽  
Author(s):  
Francis J Morgan ◽  
Geoffrey S Begg ◽  
Colin N Chesterman
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Platelet ◽  
Platelet Factor 4 ◽  
Platelet Factor ◽  
Disulphide Bonds ◽  
Covalent Structure

SummaryThe amino acid sequence of the subunit of human platelet factor 4 has been determined. Human platelet factor 4 consists of identical subunits containing 70 amino acids, each with a molecular weight of 7,756. The molecule contains no methionine, phenylalanine or tryptophan. The proposed amino acid sequence of PF4 is: Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser- Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Pro-Thr-Ala-Gin- Leu-Ile-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Leu-Gln-Ala-Pro-Leu-Tyr-Lys-Lys- Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser. From consideration of the homology with p-thromboglobulin, disulphide bonds between residues 10 and 36 and between residues 12 and 52 can be inferred.

Characterization of an isozyme of S-adenosylmethionine synthetase from rat liver

1984 ◽  
Vol 62 (5) ◽  
pp. 276-279 ◽  
Author(s):  
C. H. Lin ◽  
W. Chung ◽  
K. P. Strickland ◽  
A. J. Hudson
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Enzymatic Synthesis ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Aromatic Amino Acids ◽  
Adenosylmethionine Synthetase ◽  
Cellulose Column

An isozyme of S-adenosylmethionine synthetase has been purified to homogeneity by ammonium sulfate fractionation, DEAE-cellulose column chromatography, and gel filtration on a Sephadex G-200 column. The purified enzyme is very unstable and has a molecular weight of 120 000 consisting of two identical subunits. Amino acid analysis on the purified enzyme showed glycine, glutamate, and aspartate to be the most abundant and the aromatic amino acids to be the least abundant. It possesses tripolyphosphatase activity which can be stimulated five to six times by S-adenosylmethionine (20–40 μM). The findings support the conclusion that an enzyme-bound tripolyphosphate is an obligatory intermediate in the enzymatic synthesis of S-adenosylmethionine from ATP and methionine.

Inter-annual and seasonal dynamics of amino acid, mineral and vitamin composition of silver belly Leiognathus splendens

2014 ◽  
Vol 95 (4) ◽  
pp. 817-828 ◽  
Author(s):  
Kajal Chakraborty ◽  
Deepu Joseph
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Content ◽  
West Coast ◽  
Sensor Data ◽  
The South ◽  
Post Monsoon ◽  
South West ◽  
South West Coast ◽  
Protein Amino Acids

Silver bellies, Leiognathus splendens were studied for their spatial (south-west and south-east coasts of India), annual (2008–2011) and seasonal (pre-monsoon, monsoon and post-monsoon) variations of protein, amino acids, vitamins and minerals. The monthly mean Sea Viewing Wide Field-of-view Sensor data for the period from January 2008 to December 2011 were taken into account to indicate the distribution of the photosynthetic pigment chlorophyll-a to test the hypothesis that surface productivity might be related to nutritional biochemistry of this species. The four year average total protein content and chlorophyll-a showed good correlation during monsoon on the south-west coast and monsoon/post-monsoon on the south-east coast, suggesting that the protein content is prejudiced by the chlorophyll-a concentration. Amino acid scores observed monsoon maxima along the south-west and south-east coasts. Significant seasonal variations in vitamin content were observed at the study locations with high content of vitamins D3, E, K1 and C on the south-west coast. Na content was maximal during pre-monsoon on the south-west coast, while post-monsoon maxima of Ca and K content were observed. The Fe, Mn and Zn were abundant in the samples collected from the south-west coast. The concentration of Se exhibited maximum values post-monsoon along the south-west and south-east coasts. The present study demonstrated L. splendens as a valuable source of the protein, amino acids, minerals and vitamins, showing that this low-value species is a good source of well balanced proteins with high biological value to be qualified as a preferred healthy food for human consumption.

The C-terminal sequence of amino acid residues of κ-casein isolated from buffalo's milk

1967 ◽  
Vol 34 (1) ◽  
pp. 85-88 ◽  
Author(s):  
M. H. Abd El-Salam ◽  
W. Manson
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Peptide Chain ◽  
Amino Acid Residues ◽  
Terminal Sequence ◽  
Carboxypeptidase A ◽  
Phosphorous Content ◽  
Single Peptide

SummaryWhen κ-casein from buffalo's milk was treated with carboxypeptidase A (EC 3. 4. 2. 1),4 amino acids, valine, threonine, serine and alanine were released from the protein in a manner consistent with the view that they originate in the C-terminal sequence of a single peptide chain. The amounts produced suggest a minimum molecular weight for buffalo κ-casein of approximately 17000, in agreement with the value calculated from the phosphorous content on the basis of the presence of 2 phosphorus atoms/molecule. A comparison is made with the C-terminal sequence reported for bovine κ-casein.

scholarly journals Amino Acid Composition of Milk from Cow, Sheep and Goat Raised in Ailano and Valle Agricola, Two Localities of ‘Alto Casertano’ (Campania Region)

Foods ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 2431
Author(s):  
Nicola Landi ◽  
Sara Ragucci ◽  
Antimo Di Maro
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Protein Content ◽  
Total Protein ◽  
Free Amino ◽  
Raw Milk ◽  
Total Amino Acid ◽  
Total Protein Content ◽  
Campania Region

Cow, sheep and goat raw milk raised in Ailano and Valle Agricola territories (‘Alto Casertano’, Italy) were characterized (raw proteins, free and total amino acids content) to assess milk quality. Raw milk with the highest total protein content is sheep milk followed by goat and cow milk from both localities. Total amino acid content in cow, goat and sheep raw milk is 4.58, 4.81 and 6.62 g per 100 g, respectively, in which the most abundant amino acid is glutamic acid (~20.36 g per 100 g of proteins). Vice versa, the free amino acids content characteristic profiles are different for each species. In particular, the most abundant free amino acid in cow, sheep and goat raw milk is glutamic acid (9.07 mg per 100 g), tyrosine (4.72 mg per 100 g) and glycine (4.54 mg per 100 g), respectively. In addition, goat raw milk is a source of taurine (14.92 mg per 100 g), retrieved in low amount in cow (1.38 mg per 100 g) and sheep (2.10 mg per 100 g) raw milk. Overall, raw milk from ‘Alto Casertano’ show a high total protein content and are a good source of essential amino acids.

scholarly journals Performance of Broilers Fed Low Protein Diets with Lysine and Methionine Supplements

2006 ◽  
Vol 6 (1) ◽  
pp. 47-59
Author(s):  
Nancy Montilla ◽  
◽  
Lolito Bestil ◽  
Sulpecio Bantugan ◽  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Content ◽  
High Protein Diet ◽  
Protein Diet ◽  
Amino Acid Supplementation ◽  
Feed Conversion ◽  
Broiler Performance ◽  
Acid Supplementation ◽  
Low Protein

A feeding trial with broilers was conducted to evaluate the effects of amino acids (lysine and methionine) supplementation of diets low in protein content on the voluntary intake, feed conversion efficiency, broiler performance, and cost and return of broiler production. Results showed cumulative voluntary feed intake was not significantly affected by lowering the protein content of the diet. Cumulative weight gain of broilers was lower with diet when supplemented iwht lysine and methionine to meet requirements. Birds fed with diets low in protein has less efficient feed converstion, but became comparable with those receiveing diets high in protein when supplemented with amino acids. Feed cost per kilogram broiler produced was not significantly affected by diets used in the study, although the low-protien diet with amino acid supplement had the lowest values. In terms of return above feed and chick cost, broilers fed with high-protein diet had the greatest value, but not significantly different from birds fed with low-protien diet with amino acid supplementation which gave about P10 per bird higher returns than those fed low-protein diet without amino acid supplementation.

Isolation and characterization of some novel genes of the apolipoprotein A-I family in Japanese eel, Anguilla japonica

2011 ◽  
Vol 6 (4) ◽  
pp. 545-557 ◽  
Author(s):  
Malay Choudhury ◽  
Takahiro Oku ◽  
Shoji Yamada ◽  
Masaharu Komatsu ◽  
Keita Kudoh ◽  
...  
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Consensus Sequence ◽  
Structural Features ◽  
Lipid Binding ◽  
Japanese Eel ◽  
Amino Acid Sequences ◽  
Novel Genes ◽  
Isolation And Characterization

AbstractApolipoproteins such as apolipoprotein (apo) A-I, apoA-IV, and apoE are lipid binding proteins synthesized mainly in the liver and the intestine and play an important role in the transfer of exogenous or endogenous lipids through the circulatory system. To investigate the mechanism of lipid transport in fish, we have isolated some novel genes of the apoA-I family, apoIA-I (apoA-I isoform) 1–11, from Japanese eel by PCR amplification. Some of the isolated genes of apoIA-I corresponded to 28kDa-1 cDNAs which had already been deposited into the database and encoded an apolipoprotein with molecular weight of 28 kDa in the LDL, whereas others seemed to be novel genes. The structural organization of all apoIA-Is consisted of four exons separated by three introns. ApoIA-I10 had a total length of 3232 bp, whereas other genes except for apoIA-I9 ranged from 1280 to 1441 bp. The sequences of apoIA-Is at the exon-intron junctions were mostly consistent with the consensus sequence (GT/AG) at exon-intron boundaries, whereas the sequences of 3′ splice acceptor in intron 1 of apoIA-I1-7 were (AC) but not (AG). The deduced amino acid sequences of all apoIA-Is contained a putative signal peptide and a propeptide of 17 and 5 amino acid residues, respectively. The mature proteins of apoIA-I1-3, 7, and 8 consisted of 237 amino acids, whereas those of apoIA-I4-6 consisted of 239 amino acids. The mature apoIA-I10 sequence showed 65% identity to amino acid sequence of apoIA-I11 which was associated with an apolipoprotein with molecular weight of 23 kDa in the VLDL. All these mature apoIA-I sequences satisfied the common structural features depicted for the exchangeable apolipoproteins such as apoA-I, apoA-IV, and apoE but apoIA-I11 lacked internal repeats 7, 8, and 9 when compared with other members of apoA-I family. Phylogenetic analysis showed that these novel apoIA-Is isolated from Japanese eel were much closer to apoA-I than apoA-IV and apoE, suggesting new members of the apoA-I family.

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