Hydrogen exchange of the tryptophan residues in bovine, goat, guinea pig, and human .alpha.-lactalbumin

Biochemistry ◽  
1989 ◽  
Vol 28 (21) ◽  
pp. 8568-8576 ◽  
Author(s):  
Yoshiaki Harushima ◽  
Shintaro Sugai
Keyword(s):  
Guinea Pig ◽  
Hydrogen Exchange ◽  
Tryptophan Residues ◽  
Alpha Lactalbumin

Structure and stability of the molten globule state of guinea pig .alpha.-lactalbumin: A hydrogen exchange study

Biochemistry ◽  
1993 ◽  
Vol 32 (21) ◽  
pp. 5681-5691 ◽  
Author(s):  
Chia Lin Chyan ◽  
Claire Wormald ◽  
Christopher M. Dobson ◽  
Philip A. Evans ◽  
Jean Baum
Keyword(s):  
Guinea Pig ◽  
Hydrogen Exchange ◽  
Molten Globule ◽  
Molten Globule State ◽  
Structure And Stability ◽  
Exchange Study ◽  
Alpha Lactalbumin

scholarly journals Transgenic mice carrying the guinea-pig α-lactalbumin gene transcribe milk protein genes in their sebaceous glands during lactation

1991 ◽  
Vol 275 (2) ◽  
pp. 459-467 ◽  
Author(s):  
A Maschio ◽  
P M Brickell ◽  
D Kioussis ◽  
A L Mellor ◽  
D Katz ◽  
...  
Keyword(s):  
Gene Expression ◽  
Transgenic Mice ◽  
Guinea Pig ◽  
Milk Protein ◽  
Mouse Skin ◽  
Sebaceous Glands ◽  
Milk Protein Gene ◽  
Milk Protein Genes ◽  
Milk Protein Gene Expression ◽  
Alpha Lactalbumin

We have generated transgenic mice carrying the entire guinea-pig alpha-lactalbumin gene. Lactating transgenic mice expressed high levels of correctly initiated and processed guinea-pig alpha-lactalbumin mRNA in the secretory epithelium of their mammary glands, and secreted guinea-pig alpha-lactalbumin in their milk. Transcripts were detectable after 7 days of pregnancy, indicating that the transgene was under correct hormonal control. Whereas no or negligible transcription was detectable in all other tissues tested, high levels of transcripts were found in the skin of lactating transgenic mice. Guinea-pig alpha-lactalbumin protein was undetectable in the skin, however. In situ hybridization analysis showed that expression was localized to the undifferentiated cells in the basal layer of the sebaceous glands. Further studies revealed high levels of endogenous beta-casein mRNA in normal lactating mouse skin, demonstrating that the transcription of milk protein genes in lactating mouse skin is a normal event, and is not peculiar to the transgene. This surprising finding highlights the developmental relationship of the mammary gland to other specialized structures of the skin, supports a role for epithelial-extracellular matrix interactions in the regulation of milk protein gene expression in vivo, and identifies the skin as a particularly accessible model system in which to study the regulation of milk protein gene expression. In addition, the guinea-pig alpha-lactalbumin gene will be a source of regulatory sequences with which to direct heterologous gene expression to the sebaceous glands of transgenic mice.

Measurement of hydrogen exchange at the tryptophan residues of a protein by stopped-flow and ultraviolet spectroscopy

1978 ◽  
Vol 100 (1) ◽  
pp. 272-276 ◽  
Author(s):  
Mamoru Nakanishi ◽  
Hitomi Nakamura ◽  
Akiko Y. Hirakawa ◽  
Masamichi Tsuboi ◽  
Toshihiko Nagamura ◽  
...  
Keyword(s):  
Hydrogen Exchange ◽  
Ultraviolet Spectroscopy ◽  
Stopped Flow ◽  
Tryptophan Residues

scholarly journals Differential expression of α-lactalbumin and casein genes during the onset of lactation in the guinea-pig mammary gland

1981 ◽  
Vol 194 (3) ◽  
pp. 999-1006 ◽  
Author(s):  
L J Burditt ◽  
D Parker ◽  
R K Craig ◽  
T Getova ◽  
P N Campbell
Keyword(s):  
Mammary Gland ◽  
Guinea Pig ◽  
Post Partum ◽  
Mammary Tissue ◽  
Milk Protein Gene ◽  
Milk Protein Gene Expression ◽  
Gene Transcripts ◽  
Casein Genes ◽  
In Pregnancy ◽  
Alpha Lactalbumin

1. The expression of alpha-lactalbumin and casein genes was examined in guinea-pig mammary tissue taken from animals both pre- and post-partum. 2. Analysis of total RNA by RNA excess hybridization with sequence-specific complementary DNA probes demonstrated that alpha-lactalbumin mRNA was present late in pregnancy, and that maximum concentrations were present at parturition. Casein gene transcripts were absent late in pregnancy (62 days), but by parturition were present at concentrations identical to those found at all time points examined throughout lactation. 3. Studies using mammary explants in organ culture showed that tissue from pregnant animals, or animals at parturition, synthesized and secreted only alpha-lactalbumin. After parturition, at the onset of casein synthesis, differential rates of secretion of alpha-lactalbumin and the caseins were observed. 4. The results are discussed in terms of the multiple intracellular mechanisms involved in the regulation of milk protein gene expression in the guinea-pig mammary gland.

Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig .alpha.-lactalbumin

Biochemistry ◽  
1989 ◽  
Vol 28 (1) ◽  
pp. 7-13 ◽  
Author(s):  
Jean Baum ◽  
Christopher M. Dobson ◽  
Philip A. Evans ◽  
Claire Hanley
Keyword(s):  
Guinea Pig ◽  
Molten Globule ◽  
Molten Globule State ◽  
Nmr Methods ◽  
Alpha Lactalbumin

scholarly journals Sodium, Hydrogen exchange type 1 and bile ductular secretory activity in the guinea pig

Hepatology ◽  
2000 ◽  
Vol 31 (3) ◽  
pp. 562-571 ◽  
Author(s):  
Christian Hübner ◽  
Wolfgang Stremmel ◽  
Christoph Elsing
Keyword(s):  
Guinea Pig ◽  
Hydrogen Exchange ◽  
Secretory Activity ◽  
Sodium Hydrogen

Hydrogen exchange of the tryptophan residues in bovine ?-lactalbumin studied by uv spectroscopy

Biopolymers ◽  
1988 ◽  
Vol 27 (4) ◽  
pp. 629-644 ◽  
Author(s):  
Yoshiaki Harushima ◽  
Kunihiro Kuwajima ◽  
Shintaro Sugai
Keyword(s):  
Hydrogen Exchange ◽  
Uv Spectroscopy ◽  
Tryptophan Residues ◽  
Bovine Lactalbumin

scholarly journals Guinea-pig milk-protein synthesis. Isolation and characterization of messenger ribonucleic acids from lactating mammary gland and identification of caseins and pre-α-lactalbumin as translation products in heterologous cell-free systems

1976 ◽  
Vol 160 (1) ◽  
pp. 57-74 ◽  
Author(s):  
R K Craig ◽  
P A Brown ◽  
O S Harrison ◽  
D McIlreavy ◽  
P N Campbell
Keyword(s):  
Molecular Weight ◽  
Protein Synthesis ◽  
Mammary Gland ◽  
Guinea Pig ◽  
Wheat Germ ◽  
Milk Proteins ◽  
N Terminus ◽  
Lactating Mammary Gland ◽  
Heterologous Cell ◽  
Alpha Lactalbumin

1. The major milk proteins synthesized by the lactating mammary gland of the guinea pig were identified and designated as caseins A, B and C and alpha-lactalbumin, with estimated mol.wts. of 28000, 25500, 20500 and 14500 respectively. 2. Antisera to the total casein fraction and to alpha-lactalbumin were prepared from rabbits. The milk proteins were also iodinated with either 131I or 125I. 3. A poly(A)-rich RNA fraction was isolated from lactating guinea-pig mammary glands. Isolation was by affinity chromatography on oligo(dT)-cellulose. 4. Examination of this RNA fraction by electrophoresis on polyacrylamide gels containing formamide indicated three major species 1, 2 and 3, with estimated wol.wts. of 5.4 × 10(5) and 3.3 × 10(5), and the apparent absence of rRNA species. 5. The poly(A)-rich RNA stimulated protein synthesis in heterologous cell-free systems based on wheat germ, Krebs II ascites-tumour cells, and the latter supplemented with an initiation factor-3 fraction from rabbit reticulocyte ribosomes. 6. Between 80 and 90% of the protein synthesis directed by the mRNA was for milk proteins. 7. Analysis of the proteins immunoprecipitated by the alpha-lactalbumin antiserum showed in the wheat-germ system that the product was a protein with a molecular weight greater than that of alpha-lactalbumin, whereas in the ascites-tumour-cell systems both this protein and alpha-lactalbumin were found. When the larger protein was treated with CNBr and the resulting peptides were examined, it was shown that the extra peptide was at the N-terminus. This and other evidence is adduced for the initial translation product of alpha-lactalbumin being a precursor with an addition of about ten amino acids at the N-terminus. 8. Similar analysis of the casein immlnospecific proteins produced under the direction of mRNA indicated that the products had a molecular weight that was apparently a littel smaller than that of the caseins synthesized in vivo. This was not consistent with higher-molecular weight casein precursors. 9. Possible explanations for the results obtained are discussed, especially in terms of the physiological significance of the pre-alpha-lactalbumin as a secretory protein.

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