Molecular organization of the human cathepsin D gene.

A 16-kb fragment of human DNA containing the cathepsin D (CATD) gene was isolated. Nucleotide sequencing, primer extension, protection from mung bean nuclease, and promoter activity assays were used to characterize the gene. The transcribed portion of the gene is about 11,000 bp and is organized into 9 exons analogous with the human pepsinogen A gene.

UGA is translated as cysteine in pheromone 3 of Euplotes octocarinatus.

Pheromone 3 mRNA of the ciliate Euplotes octocarinatus contains three in-frame UGA codons that are translated as cysteines. This was revealed from cDNA sequencing and from plasma desorption mass spectrometry of cleaved pheromone 3 in connection with pyridylethylation of the fragments. N-terminal sequence analysis of carboxymethylated protein confirmed this conclusion for the first of the three UGA codons.

Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment.

A 2112-bp cDNA clone (lambda CT29) encoding the entire sequence of the human lysosomal acid phosphatase (EC 3.1.3.

Cloning of a cDNA encoding the human cation-dependent mannose 6-phosphate-specific receptor.

Complementary DNA clones for the human cation-dependent mannose 6-phosphate-specific receptor have been isolated from a human placenta library in lambda gt11. The nucleotide sequence of the 2463-base-pair cDNA insert includes a 145-base-pair 5' untranslated region, an open reading frame of 831 base pairs corresponding to 277 amino acids (Mr = 30,993), and a 1487-base-pair 3' untranslated region. The deduced amino acid sequence is colinear with that determined by amino acid sequencing of the N-terminus peptide (41 residues) and nine tryptic peptides (93 additional residues).

Influence of effectors of the complex-type-oligosaccharide biosynthesis on the formation of proteokeratan sulfate in bovine cornea.

The structural similarity of the inner core of complex-type prosthetic oligosaccharides of N-asparagine glycoproteins and of the linkage region between the polysaccharide part and the protein chain of cornea proteokeratan sulfate makes their biosynthesis via a common route an attractive hypothesis. To test this, a tissue culture system was established to determine the rate of proteokeratan sulfate biosynthesis in bovine cornea and to measure the influence of several effectors of the dolichol pathway on this rate. Addition of dolichyl phosphate enhanced the formation of proteokeratan sulfate.