A NEUROPHYSIN FROM COD (GADUS MORRHUA) PITUITARY GLANDS: ISOLATION AND PROPERTIES

1968 ◽  
Vol 42 (1) ◽  
pp. 143-NP ◽  
Author(s):  
B. T. PICKERING
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Composition ◽  
Arginine Vasopressin ◽  
Binding Capacity ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Maximum Binding Capacity ◽  
Pituitary Glands

SUMMARY A protein capable of binding neurohypophysial hormones has been isolated from cod pituitary glands using gel filtration and ion-exchange chromatography. The cod protein which was acidic and rich in cystine had an amino acid composition closely related to those of the mammalian neurophysins. It had a maximum binding capacity of 2·2 μmole/14mg. for oxytocin, 2·1 μmole/14 mg. for [8-arginine]-oxytocin and 1·1 μmole/14 mg. for [8-arginine]-vasopressin. Thus the cod protein had a greater capacity for the endogenous pressor-antidiuretic peptide than for the analogous mammalian hormone.

scholarly journals Isolation and a partial amino acid sequence of insulin from the islet tissue of cod (Gadus callarias)

1968 ◽  
Vol 106 (2) ◽  
pp. 531-541 ◽  
Author(s):  
P T Grant ◽  
K. B. M. Reid
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Gel Filtration ◽  
Bovine Insulin ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Performic Acid ◽  
Amino Acid Residues ◽  
Islet Tissue ◽  
A Chain

1. Insulin has been isolated by gel filtration and ion-exchange chromatography from extracts of the discrete islet tissue of cod. The final preparation yielded a single band on electrophoresis at two pH values. The biological potency was 11·5 international units/mg. in mouse-convulsion and other assay procedures. 2. Glycine and methionine were shown to be the N-terminal amino acids of the A and B chains respectively. An estimate of the molecular weight together with amino acid analyses indicated that cod insulin, like the bovine hormone, consists of 51 amino acid residues. In contrast, the amino acid composition differs markedly from bovine insulin. 3. Oxidation of insulin with performic acid yielded the A and B peptide chains, which were separated by ion-exchange chromatography. Sequence studies on smaller peptides isolated from enzymic digests or from dilute acetic acid hydrolysates of the two chains have established the sequential order of 14 of the 21 amino acid residues of the A chain and 25 of the 30 amino acid residues of the B chain.

scholarly journals Studies on Marsupial Protein. II. Amino Acid Sequence of the -Chain of Haemoglobin from the Grey Kangaroo, Macropus Giganteus

1969 ◽  
Vol 22 (6) ◽  
pp. 1437 ◽  
Author(s):  
GM Air ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Sequence ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
Tryptic Digestion ◽  
Grey Kangaroo

The amino acid sequence of the jS-chain of haemoglobin from M. giganteus has been determined. The soluble peptides formed by tryptic digestion were isolated by gel filtration, ion-exchange chromatography, and paper ionophoresis, and amino acid sequences determined by the "dansyl"-Edman procedure. Special procedures were necessary for three peptides which were insoluble.

scholarly journals High-Sulphur Proteins From a-Keratins ll. Isolation and Partial Characterization of Purified Components From Mouse Hair

1976 ◽  
Vol 29 (2) ◽  
pp. 11 ◽  
Author(s):  
Robert C Marshall ◽  
JM Gillespie
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Fractional Precipitation ◽  
Molecular Weight Range

The present paper continues the study of the reduced and S-carboxymethylated high-sulphur proteins from mouse hair. Fractions have been obtained in a substantially purified form by fractional precipitation with ammonium sulphate at pH 6, followed by ion exchange chromatography on cellulose phosphate at pH 2�6. Approximately 80% by weight of the high-sulphur proteins fall into the ultra-high-sulphur category (carboxymethyicysteine content greater than 26 residues per 100 residues), and they cover a molecular weight range of 17000-28000. The components show a remarkable diversity in amino acid composition; for example the contents of arginine and glycine each vary by about 3 : 1. The remainder of the proteins contain 17-20 residues per 100 residues of carboxymethyicysteine, are smaller in size (molecular weight 11 500), and also show great diversity in overall amino acid composition.

PURIFICATION OF HUMAN PARATHYROID HORMONE: RECENT STUDIES AND FURTHER OBSERVATIONS

1978 ◽  
Vol 78 (1) ◽  
pp. 49-58 ◽  
Author(s):  
H. T. KEUTMANN ◽  
G. N. HENDY ◽  
M. BOEHNERT ◽  
J. L. H. O'RIORDAN ◽  
J. T. POTTS
Keyword(s):  
Parathyroid Hormone ◽  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Trichloroacetic Acid ◽  
Gel Filtration ◽  
Exchange Chromatography ◽  
Human Parathyroid Hormone ◽  
Successive Extraction

During the isolation of human parathyroid hormone there is an extensive loss of immunoassayable hormone over the successive extraction steps, due in part to the presence of fragments that are soluble in 4% trichloroacetic acid. These fragments are derived from both the amino- and carboxyl-terminal regions of the hormone. The hormonal fractions precipitated with trichloroacetic acid were further purified by gel filtration and ion-exchange chromatography. At the final ion-exchange purification step, some preparations of the hormone eluted in multiple fractions. When the various components were characterized separately by immunoassay, amino acid composition, enzymic cleavage and partial sequence analysis, they were found to be closely comparable, although the most acidic fraction contained a blocked terminal amino group. Extraction of a number of batches of tissue permitted revision of the amino acid composition of human parathyroid hormone. Biosynthetic studies with labelled amino acids confirmed the absence of tyrosine and the presence of phenylalanine and threonine and localized these residues to definite regions of the molecule.

scholarly journals Myoglobins of Cartilaginous Fishes III. Amino Acid Sequence of Myoglobin of the Shark Galeorhinus Australis

1981 ◽  
Vol 34 (1) ◽  
pp. 5 ◽  
Author(s):  
WK Fisher ◽  
DD Koureas ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Sequence ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Red Muscle ◽  
Cartilaginous Fishes ◽  
Port Jackson

Myoglobin isolated from the red muscle of the school shark Galeorhinus australis was purified by gel filtration and ion-exchange chromatography. The amino acid sequence was determined following digestion with trypsin and purification of the peptides by paper ionophoresis and chromatography. Sequences of purified peptides were determined by the dansyl-Edman procedure and the peptides aligned by homology with the sequence of the myoglobin of the gummy shark Mustelus antarcticus. The two myoglobin sequences showed a marked similarity (16 differences), but both sequences showed approximately the same number of differences (68) from myoglobin of the Port Jackson shark Heterodontus portusjacksoni. There are 19 residues unique to the three shark myoglobin sequences.

scholarly journals The Amino Acid Composition of hydrolysates of Microbial Preparations From the Rumen of Sheep

1957 ◽  
Vol 10 (3) ◽  
pp. 384 ◽  
Author(s):  
RA Weller
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Different Types

Samples of bacteria and of protozoa were separated from the rumen fluids of sheep which had been fed four different types of ration. Amino acid analyses by ion-exchange chromatography were performed on hydrolysates of "whole protein" preparations of the microbial fractions.

Bilirubin binding capacity of albumin isolated from cord-blood serum is less than that from serum of adults.

1980 ◽  
Vol 26 (6) ◽  
pp. 738-740 ◽  
Author(s):  
A Alayoff ◽  
J Kapitulnik ◽  
A Konijn ◽  
N A Kaufmann ◽  
S H Blondheim
Keyword(s):  
Ion Exchange ◽  
Blood Serum ◽  
Cord Blood ◽  
Binding Capacity ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Cord Blood Serum ◽  
Bilirubin Binding

Abstract As estimated by Sephadex gel filtration, the bilirubin binding capacity of albumin isolated from cord-blood serum by ion-exchange chromatography is less than that of albumin isolated from serum of adults. Albumin isolated from cord-blood serum showed increased bilirubin binding as compared with the albumin in the native serum. These findings suggest that the lower bilirubin binding capacity of serum from newborns as compared with serum from adults is a result of both an intrinsic deficiency in binding capacity of neonatal albumin and the presence of substances in neonatal serum that interfere with bilirubin binding.

Bilirubin binding capacity of albumin isolated from cord-blood serum is less than that from serum of adults.

1980 ◽  
Vol 26 (6) ◽  
pp. 738-740
Author(s):  
A Alayoff ◽  
J Kapitulnik ◽  
A Konijn ◽  
N A Kaufmann ◽  
S H Blondheim
Keyword(s):  
Ion Exchange ◽  
Blood Serum ◽  
Cord Blood ◽  
Binding Capacity ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Cord Blood Serum ◽  
Bilirubin Binding

Abstract As estimated by Sephadex gel filtration, the bilirubin binding capacity of albumin isolated from cord-blood serum by ion-exchange chromatography is less than that of albumin isolated from serum of adults. Albumin isolated from cord-blood serum showed increased bilirubin binding as compared with the albumin in the native serum. These findings suggest that the lower bilirubin binding capacity of serum from newborns as compared with serum from adults is a result of both an intrinsic deficiency in binding capacity of neonatal albumin and the presence of substances in neonatal serum that interfere with bilirubin binding.

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