Human pituitary thyrotropin. Isolation and characterization of the hormone and its subunits

1977 ◽  
Vol 55 (7) ◽  
pp. 747-754 ◽  
Author(s):  
M. R. Sairam ◽  
Choh Hao Li
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Disc Electrophoresis ◽  
Carbohydrate Content ◽  
Human Pituitary ◽  
Terminal Residue ◽  
Isolation And Characterization

Procedures have been described for the isolation of highly purified thyrotropin from frozen or acetone-preserved glands or from side fractions of somatotropin isolation and for the separation of its α and β subunits. The products have been characterized by terminal residue analyses, amino acid composition, carbohydrate content, disc electrophoresis, ultracentrifugation, and biological activity.

Isolation and characterization of a peptide derived from the active site of chicken pepsin

1980 ◽  
Vol 45 (7) ◽  
pp. 2131-2134 ◽  
Author(s):  
Helena Keilová ◽  
Vladimír Kostka ◽  
Miroslav Baudyš
Keyword(s):  
Amino Acid ◽  
Methyl Ester ◽  
Amino Acid Composition ◽  
Aspartic Acid ◽  
Acid Composition ◽  
Active Site ◽  
Its Sequence ◽  
Aspartic Acid Residue ◽  
Isolation And Characterization

A peptide was isolated from chicken pepsin which contains the aspartic acid residue reacting with diazoacetyl-D,L-norleucine methyl ester in the presence of Cu2+ -ions. The peptide is N-terminated with isoleucine and contains (besides isoleucine) valine, aspartic acid, two threonines, serine, and leucine. In concurrent experiments a peptide of the same composition was isolated from the thermolysin digest of chicken pepsin and its sequence determined as Ile-Val-Asp-Thr-Gly-Thr-Ser-Leu. Since both peptides have entirely identical amino acid composition and other characteristics, the sequenced peptide corresponds to the peptide isolated from the active site of the enzyme.

scholarly journals ISOLASI DAN KARAKTERISASI KOLAGEN DARI KULIT IKAN PATIN (Pangasius sp.)

2018 ◽  
Vol 8 (1) ◽  
pp. 8 ◽  
Author(s):  
Pipih Suptijah ◽  
Dini Indriani ◽  
Supriyono Eko Wardoyo
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Ph Value ◽  
Helical Structure ◽  
Color Analysis ◽  
Alternative Source ◽  
Isolation And Characterization ◽  
Naoh Solution

Isolation and Characterization of Collagen from the Skin of Catfish (Pangasius sp.)           Skin of catfish is one of aquatic by-products which could be used as an alternative source of collagen. This research is aimed to isolate and characterize collagen from skin of catfish. Methods of  isolation of collagen included three stages, the first was deproteinization using NaOH solution with concentration of 0.05 M; 0.10 M; 0.15 M; 0.20 M for 12 hours, the second was soaking in CH3COOH solution with concentration of 0.05 M; 0.10 M; 0.15 M; and 0.20 M for 2 hours, and the third was extraction in water at a temperature of 40 0C for 2 hours; characterization of collagen was included chemical and physical properties. The results showed that the best extraction method ofcollagen from skin of catfish was soaking the skin in 0.05 M NaOH solution for 12 hours and soaking the skin in 0.05 M acetic acid for 2 hours. Extraction yields of collagen was 12.15%. Chemical characteristics included proximate and amino acid composition. Proximate value of collagen consisted of moisture was 6.55%, ash 1.80%,  protein 64.74% and fat 8.85%.  The major amino acid composition of collagen were glycine, proline, alanine, arginine and glutamate. Physical characteristics of collagen resulted from FTIR analysis showed amide A, amide B, amide I, amide II and amide III, triple helical structure of the amide I and amide III indicates that the compound produced was collagen; color analysis was 66.39%; thermal analysis showed a melting temperature peak was 154.47 0C and pH value was 5.34.Keywords : Catfish, isolation, characterization, collagen, skin ABSTRAK          Kulit ikan patin merupakan salah satu limbah hasil perairan yang dapat digunakan sebagai sumber alternatif kolagen. Penelitian ini bertujuan untuk mengisolasi dan karakterisasi kolagen yang diperoleh dari kulit ikan patin. Isolasi kolagen yang dilakukan meliputi tiga tahap, yaitu tahap pertama adalah proses deproteinisasi menggunakan larutan NaOH dengan konsentrasi, yaitu 0,05 M; 0,10 M; 0,15 M; 0,20 M dan lama waktu perendaman selama 12 jam; tahap kedua, yaitu perendaman dalam larutan CH3COOH dengan empat konsentrasi CH3COOH yaitu 0,05 M; 0,10 M; 0,15 M; dan 0,20 M dan lama waktu perendaman selama 2 jam; dan tahap ketiga, yaitu ekstraksi dengan air pada suhu 40 0C selama 2 jam; serta karakterisasi kolagen yang dilakukan, meliputi sifat kimia dan fisik. Hasil penelitian menunjukkan bahwa metode ekstraksi kolagen dari kulit ikan patin  terbaik diperoleh melalui proses perendaman kulit dalam larutan NaOH 0,05 M selama 12 jam dan  perendaman kulit dalam asam asetat 0,05 M selama 2 jam.  Rendemen serbuk kolagen yang dihasilkan sebesar 12,15 %. Karakteristik kimia meliputi proksimat dan komposisi asam amino. Nilai proksimat kolagen terdiri dari kadar air 6,55 %,  abu 1,80 %, protein 64,74 % dan lemak 8,85 %. Komposisi asam amino yang dominan pada kolagen adalah glisina, prolina, alanina, arginina dan glutamat. Karakteristik fisik kolagen yang dihasilkan adalah analisis FTIR menunjukkan adanya gugus amida A, amida B, amida I, amida II dan amida III, struktur triple heliks pada amida I dan amida III mengindikasikan bahwa senyawa yang dihasilkan adalah kolagen; analisis warna  yaitu 66,39 %; analisis termal yang menunjukkan suhu puncak pelelehan adalah 154,47 0C dan nilai pH kolagen yaitu 5,34. Kata kunci : Ikan patin, isolasi, karakterisasi, kolagen, kulit 

scholarly journals The isolation and characterization of bovine C4a, an activation fragment of the fourth component of complement

1979 ◽  
Vol 183 (3) ◽  
pp. 573-578 ◽  
Author(s):  
N A Booth ◽  
R D Campbell ◽  
M A Smith ◽  
J E Fothergill
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Complement C4 ◽  
Alpha Chain ◽  
Isolation And Characterization ◽  
Fourth Component

The fourth component of bovine complement, C4, was cleaved specifically by subcomponent C1s to produce two fragments, C4a and C4b. The smaller, C4a, was isolated in pure form and is a peptide of 9500 mol.wt. containing approx. 84 amino acids and no detectable carbohydrate. C4a has an amino acid composition that is comparable with the anaphylatoxins C3a and C5a, containing six cysteine residues/mol and a high proportion of basic residues. The amino acid sequence of the first thirteen residues shows four identities with the porcine C3a sequence. There is almost complete identity between the C4a sequence and that of the alpha-chain of human C4, indicating that this region is highly conserved. This evidence also clearly establishes that C4a is cleaved from the N-terminal of the alpha-chain of C4.

The characterization of the 12 S "globulin" from rapeseed and its glycoprotein component

1970 ◽  
Vol 48 (10) ◽  
pp. 1096-1103 ◽  
Author(s):  
L. A. Goding ◽  
R. S. Bhatty ◽  
A. J. Finlayson
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Sedimentation Coefficient ◽  
Carbohydrate Content ◽  
Amino Terminal ◽  
Terminal Amino

A 12 S globulin was isolated from each of the two species of rapeseed (B. napus L. and B. campestris L.) and they have been shown to be similar in terms of amino acid composition, amino terminal amino acids, number of subfractions, and carbohydrate content. One of the major proteins, a glycoprotein, present in each of the 12 S aggregates, was isolated and purified. Its amino acid composition, carbohydrate content, N-terminal amino acids, and sedimentation coefficient are reported herein.

scholarly journals Action of human lysosomal elastase on the oxidized B chain of insulin

1977 ◽  
Vol 161 (1) ◽  
pp. 13-16 ◽  
Author(s):  
A M J Blow
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Human Neutrophil ◽  
British Library ◽  
Carboxyl Group ◽  
Pancreatic Elastase ◽  
Terminal Residue

The specificity of action of the lysosomal elastase of human neutrophil leucocytes on the oxidized B chain of insulin is similar to that of pig pancreatic elastase, but is more directed towards valine than alanine as the residue contributing the carboxyl group of the cleaved bond. The most susceptible bonds are Val-12-Glu-13 and Val-18-Cys(O3H)-19. Other bonds hydrolysed are Ala-14-Leu-15, Ser-9-His-10 and Cys, (O3H3)-7-Gly-8. Tables listing amino acid composition, N-terminal residue, and yields of isolated peptides have been deposited as Supplementary Publication SUP 50 075 (8 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1977) 161, 1.

Amino acid composition of salmon calcitonin

1969 ◽  
Vol 47 (8) ◽  
pp. 823-825 ◽  
Author(s):  
R. K. O'Dor ◽  
C. O. Parkes ◽  
D. H. Copp
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Salmon Calcitonin ◽  
Ultimobranchial Glands

Calcitonin has been extracted from salmon ultimobranchial glands and purified. The amino acid composition indicates similarities to mammalian calcitonin but the salmon hormone has 25 times the biological activity of the most active mammalian material.

scholarly journals Purification and biochemical characterization of three major acidic proteins (BSP-A1, BSP-A2 and BSP-A3) from bovine seminal plasma

1987 ◽  
Vol 241 (3) ◽  
pp. 685-692 ◽  
Author(s):  
P Manjunath ◽  
M R Sairam
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Seminal Plasma ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Polyacrylamide Gel ◽  
Terminal Residue ◽  
Acidic Proteins

Three major acidic proteins of bovine seminal plasma, BSP-A1, BSP-A2 and BSP-A3, were purified to homogeneity, by employing fast protein liquid chromatography, gel filtration and h.p.l.c. The proteins were purified on the basis of their stimulatory effect on the basal release of gonadotropins by rat anterior-pituitary cells in culture. All three proteins migrated as distinct single bands in the presence or absence of 2-mercaptoethanol in SDS/polyacrylamide-gel electrophoresis. Their Mr values were estimated to be between 15,000 and 16,500 by SDS/polyacrylamide-gel electrophoresis. Similar Mr estimates were obtained when they were subjected to gel filtration on a calibrated column of Sephadex G-75 equilibrated in 0.05 M-acetic acid, pH 3.0. However, BSP-A1 and BSP-A2 were eluted as aggregated molecules (Mr 60,000-120,000) during gel filtration on Sephadex G-200 equilibrated in 0.05 M-NH4HCO3, pH 8.5, or phosphate buffer, pH 7.0, containing 0.15 M-NaCl. In the presence of 8 M-urea both BSP-A1 and BSP-A2 were eluted at positions corresponding to Mr values of 17,000-20,000. BSP-A1 and BSP-A2 had an identical amino acid composition, which differed largely from that of BSP-A3. All three proteins contained aspartic acid as the N-terminal residue, and cysteine was identified as the C-terminal residue. BSP-A1 and BSP-A2 are glycoproteins containing galactosamine, sialic acid and neutral sugars, but BSP-A3 did not contain any covalently attached sugars. Whereas BSP-A2 and BSP-A3 were eluted unadsorbed, BSP-A1 bound to wheat-germ lectin-Sepharose 6MB and could be eluted by the competing sugar N-acetyl-D-glucosamine. Treatment of BSP-A1 and BSP-A2 with trypsin resulted in complete loss of gonadotropin-release activity, but BSP-A3 retained full activity. Antibody raised against BSP-A1 did not cross-react with BSP-A3, or vice versa. All these properties indicated marked structural differences between BSP-A3 and BSP-A1 (or BSP-A2). On the basis of amino acid composition it was concluded that BSP-A1, BSP-A2 and BSP-A3 are the same as the gonadostatins [Esch, Ling, Bohlen, Ying & Guillemin (1983) Biochem. Biophys. Res. Commun. 113, 861-867].

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