Molecular cloning of cDNAs for precursors of porcine pituitary glycoprotein hormone common alpha-subunit and of thyroid stimulating hormone beta-subunit

التفاصيل البيبلوغرافية
العنوان: Molecular cloning of cDNAs for precursors of porcine pituitary glycoprotein hormone common alpha-subunit and of thyroid stimulating hormone beta-subunit
المؤلفون: Hirai Toshiaki, Takikawa Hiroo, Kato Yukio
المصدر: Molecular and cellular endocrinology. 63(1-2)
سنة النشر: 1989
مصطلحات موضوعية: Untranslated region, Swine, Molecular Sequence Data, Thyrotropin, Biology, Biochemistry, Endocrinology, Complementary DNA, Coding region, Animals, Amino Acid Sequence, Cloning, Molecular, Protein Precursors, Molecular Biology, Peptide sequence, chemistry.chemical_classification, Messenger RNA, Base Sequence, cDNA library, Nucleic acid sequence, DNA, Molecular biology, Amino acid, chemistry, Glycoprotein Hormones, alpha Subunit
الوصف: cDNA clones encoding precursors of glycoprotein hormone common alpha-subunit (pre-alpha) and of thyroid stimulating hormone beta-subunit (pre-TSH beta) were isolated from a porcine anterior pituitary cDNA library using DNA probes, and the nucleotide sequences were determined. The nucleotide sequence of pre-alpha cDNA contained an entire coding region (360 bases) including 5' and 3' untranslated regions. The pre-alpha mRNA was about 900 bases long. The predicted amino acid sequence consisted of a signal peptide of 24 amino acid residues and a mature alpha-subunit protein of 96 residues. Six amino acid residues at the amino terminus of the predicted mature protein had not been found by direct amino acid sequencing of the purified protein. The nucleotide sequence of pre-TSH beta cDNA contained an entire coding region and a 3' untranslated region which has two polyadenylation signals. The length of the pre-TSH beta mRNA was about 500 bases long. The predicted amino acid sequence consisted of a signal peptide of 20 amino acid residues, a mature protein of 112 residues and an additional extension of six amino acid residues at the carboxyl terminus, which had not been found in the amino acid sequence of the purified protein. The coding sequences of the cDNAs showed high homologies with those of other mammalian species (84-93% for pre-alpha and 81-94% for pre-TSH beta). Comprehensive data of our serial molecular cloning for porcine glycoprotein hormones revealed low but significant homologies (34-40%) among three beta-subunits. Upon comparison of frequency of (U)n A sequence in 3' untranslated region, porcine pre-alpha and pre-TSH beta mRNAs were grouped into a moderate class of mRNA stability whereas porcine pre-FSH beta and pre-LH beta were grouped into unstable and stable classes, respectively.
تدمد: 0303-7207
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7b981d3f0e6ee3542c8d3c9cb1a0db9Test
https://pubmed.ncbi.nlm.nih.gov/2473932Test
حقوق: CLOSED
رقم الانضمام: edsair.doi.dedup.....f7b981d3f0e6ee3542c8d3c9cb1a0db9
قاعدة البيانات: OpenAIRE