scholarly journals Preparation and properties of creatine kinase from the breast muscle of normal and dystrophic chicken (Gallus domesticus)

1970 ◽  
Vol 120 (1) ◽  
pp. 177-185 ◽  
Author(s):  
B. P. Roy ◽  
J. F. Laws ◽  
A. R. Thomson
Keyword(s):  
Creatine Kinase ◽  
Amino Acid ◽  
Amino Acid Sequences ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Kinetic Properties ◽  
Thiol Groups ◽  
Dystrophic Muscle ◽  
Peptide Maps ◽  
Dystrophic Chicken

1. The purification of creatine kinase from normal and genetically dystrophic chicken breast muscle is described. Enzyme recovery was significantly lower from dystrophic muscle. 2. Both enzymes had the same number of reactive and total thiol groups and had similar specific activities and similar amino acid compositions. 3. No significant differences were observed in sedimentation, electrophoretic or kinetic properties. 4. Peptide `maps' showed no significant differences, and electrophoresis of partial acid hydrolysates of the labelled enzymes suggested that corresponding amino acid sequences around all the thiol groups were very similar. 5. The enzymes showed identical temperature stabilities. 6. No significant differences between the enzymes from normal and dystrophic muscle were observed.

scholarly journals The amino acid sequence of the peptide containing the thiol group of creatine kinase from normal and dystrophic chicken breast muscle. Comparison of some of the immunological properties of the antibodies developed in rabbits against these enzymes

1974 ◽  
Vol 143 (1) ◽  
pp. 171-179 ◽  
Author(s):  
Buddha P. Roy
Keyword(s):  
Creatine Kinase ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Thiol Group ◽  
Chicken Breast ◽  
Thiol Groups ◽  
Dystrophic Muscle ◽  
Muscle Enzymes ◽  
Chicken Muscle ◽  
Dystrophic Chicken

The major14C-labelled peptides from creatine kinase from normal and dystrophic chicken muscle obtained by carboxymethylating the reactive thiol groups with iodo[2-14C]acetic acid and digestion with trypsin were purified by ion-exchange chromatography on Dowex-50 (X2) and by paper electrophoresis. The chromatographic characteristics of the14C-labelled peptides, their electrophoretic mobilities at pH6.5, and their amino acid compositions were identical for the two enzymes. The sequence of amino acids around the essential thiol groups of creatine kinase from normal and dystrophic chicken muscle was shown to be Ile-Leu-Thr-CmCys-Pro-Ser-Asn-Leu-Gly-Thr-Gly-Leu-Arg (CmCys, carboxymethylcysteine). This sequence is almost identical with that for the creatine kinases in human and ox muscle and bovine brain and is very similar to that of arginine kinase from lobster muscle. Antibodies to the enzymes were raised in rabbits and their reaction with the creatine kinase from normal and dystrophic muscles in interfacial, immunodiffusion and immunoelectrophoretic experiments was studied. The cross-reaction between normal muscle creatine kinase and antisera against the dystrophic muscle enzyme (or vice versa) observed by immunodiffusion and by immunoelectrophoretic experiments further suggests that the enzymes from normal and dystrophic chicken muscle are similar in structure. The results of the present study, the identical amino acid sequence of the peptides containing the reactive thiol group from both the normal and dystrophic chicken muscle enzymes and the immunological similarities of the two enzymes are in accord with the similarity of the two enzymes observed by Roy et al. (1970).

scholarly journals Selective purification of the thiol peptides of myosin

1968 ◽  
Vol 107 (4) ◽  
pp. 531-548 ◽  
Author(s):  
A G Weeds ◽  
B S Hartley
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Performic Acid ◽  
Cysteic Acid ◽  
Acid Oxidation ◽  
Thiol Groups ◽  
Peptide Maps ◽  
Thiol Peptides

1. A method for selective purification of thiol peptides is described. Thiol groups in a protein are treated with radioactive cystine by disulphide–thiol interchange. The labelled cystine peptides in a digest can then be fractionated for peptide ‘maps’. Performic acid oxidation of paper strips containing the radioactive peptides followed by further ionophoresis yields the purified cysteic acid peptides. 2. The thiol peptides in a peptic digest of cystine-exchanged myosin were purified in this way, and their amino acid sequences were determined. 3. The conclusion that myosin contains at least 16, and probably between 20 and 22, unique thiol sequences indicates that the molecule consists of two chemically equivalent components.

scholarly journals A novel giant secretion polypeptide in Chironomus salivary glands: implications for another Balbiani ring gene.

1985 ◽  
Vol 101 (3) ◽  
pp. 1044-1051 ◽  
Author(s):  
W Y Kao ◽  
S T Case
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Salivary Glands ◽  
Cyanogen Bromide ◽  
Tryptic Peptide ◽  
Amino Acid Sequences ◽  
The Other ◽  
Balbiani Ring ◽  
Sequence Organization ◽  
Peptide Maps

Chironomus salivary glands contain a family of high Mr (approximately 1,000 X 10(3)) secretion polypeptides thought to consist of three components: sp-Ia, sp-Ib, and sp-Ic. The use of a new extraction protocol revealed a novel high Mr component, sp-Id. Results of a survey of individual salivary glands indicated that sp-Id was widespread in more than a dozen strains of C. tentans and C. pallidivittatus. Sp-Id was phosphorylated at Ser residues, and a comparison of cyanogen bromide and tryptic peptide maps of 32P-labeled polypeptides suggested that sp-Ia, sp-Ib, and sp-Id are comprised of similar but nonidentical tandemly repeated amino acid sequences. We concluded that sp-Id is encoded by an mRNA whose size and nucleotide sequence organization are similar to Balbiani ring (BR) mRNAs that code for the other sp-I components. Furthermore, parallel repression of sp-Ib and sp-Id synthesis by galactose led us to hypothesize that both of their genes exist within Balbiani ring 2.

Comparison of the structural and kinetic properties of the cytochrome c nitrite reductases from Escherichia coli, Wolinella succinogenes, Sulfurospirillum deleyianum and Desulfovibrio desulfuricans

2006 ◽  
Vol 34 (1) ◽  
pp. 143-145 ◽  
Author(s):  
T.A. Clarke ◽  
A.M. Hemmings ◽  
B. Burlat ◽  
J.N. Butt ◽  
J.A. Cole ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Active Site ◽  
Desulfovibrio Desulfuricans ◽  
Amino Acid Sequences ◽  
Kinetic Properties ◽  
Wolinella Succinogenes ◽  
Nitrite Reductases ◽  
Sulphite Reductase

The recent crystallographic characterization of NrfAs from Sulfurospirillum deleyianum, Wolinella succinogenes, Escherichia coli and Desulfovibrio desulfuricans allows structurally conserved regions to be identified. Comparison of nitrite and sulphite reductase activities from different bacteria shows that the relative activities vary according to organism. By comparison of both amino acid sequences and structures, differences can be identified in the monomer–monomer interface and the active-site channel; these differences could be responsible for the observed variance in substrate activity and indicate that subtle changes in the NrfA structure may optimize the enzyme for different roles.

scholarly journals Two tissue-specific isozymes of creatine kinase have closely matched amino acid sequences.

1985 ◽  
Vol 82 (8) ◽  
pp. 2310-2314 ◽  
Author(s):  
L. Pickering ◽  
H. Pang ◽  
K. Biemann ◽  
H. Munro ◽  
P. Schimmel
Keyword(s):  
Creatine Kinase ◽  
Amino Acid ◽  
Amino Acid Sequences ◽  
Tissue Specific

scholarly journals Amino acid sequences aroung the thiol groups of myokinase

1968 ◽  
Vol 107 (2) ◽  
pp. 311-312 ◽  
Author(s):  
A G Weeds ◽  
L Noda
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Thiol Groups

scholarly journals The amino acid profile after addition of humic acids and phytobiotics into diet of broiler chicken

10.5219/1237 ◽  
2019 ◽  
Vol 13 (1) ◽  
pp. 884-890
Author(s):  
Peter Haščík ◽  
Adriana Pavelková ◽  
Jana Tkáčová ◽  
Juraj Čuboň ◽  
Marek Bobko ◽  
...  
Keyword(s):  
Amino Acid ◽  
Humic Acids ◽  
Broiler Chickens ◽  
Broiler Chicken ◽  
Amino Acid Profile ◽  
Breast Muscle ◽  
Thigh Muscle ◽  
Chicken Breast ◽  
Control Group ◽  
Garlic Powder

The aim of the study was analysed the effect of humic acids separately and humic acids in combination with phytobiotic as garlic and oregano powder on amino acid (AA) profile of the most valuable parts of Ross 308 chicken. A total of 200 pcs Ross 308 broiler chickens of mixed sex were randomly divided into 4 groups (n=50): control group (C) without supplementation, experiment group E1 (2% humic acids), E2 (80% humic acids and 20% garlic powder) and E3 (90% humic acids and 10% oregano powder). Fattening period lasted for 42 days and all groups were kept under the same conditions. After slaughter, the AA profiles of breast and thigh samples were determined. In comparison with control group, 6 out of 10 AA was significantly affected (p ≤0.05) by used dietary supplementation – Met, Cys and His in thigh and Leu, Phe, His and Arg in breast muscle. AA composition of breast muscle was positively affected mainly by humic acids and 10% oregano powder supplementation (E3), while thigh muscle by humic acids and 20% garlic powder (E2). The highest obtained AA in breast muscle was Leu (2.02 g.100 g-1) in E3 group and thigh muscle His (1.15 g.100 g-1) in E2 group (p ≤0.05). In conclusion, humic acids and 10% oregano powder supplementation (E3) elicited to the best AA profile of chicken breast muscle but also the worst AA profile in thigh muscle so the effect of such a supplementation is disputable. On the other hand, humic acids and 20% garlic powder supplementation resulted into slight increase of AA in both breast and thigh muscle (E2).

scholarly journals Amino Acid Sequences Containing Half-Cystine Residues in Ovalbumin

1978 ◽  
Vol 31 (5) ◽  
pp. 433 ◽  
Author(s):  
EOP Thompson ◽  
WK Fisher
Keyword(s):  
Amino Acid ◽  
Disulfide Bond ◽  
Amino Acid Sequences ◽  
Thiol Groups

Ovalbumin is known to have six half-cystine residues with four thiol groups and one disulfide bond.

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