Jonathan Hanes

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The characterization of major proteins of honeybee larval jelly (49 – 87 kDa) was performed by the sequencing of new complementary DNAs (cDNAs) obtained from a honeybee head cDNA library, by the determination of N-terminal sequences of the proteins, and by analyses of the newly obtained and known sequence data concerning the proteins. It was found that(More)
Two new human cDNAs, designated phclk2 and phclk3, which have a high identity to the cDNA of the human protein kinase clk, were characterized. Typical features of hclk2 and hclk3 proteins are non-homologous N-terminal regions and the presence of the C-terminal protein kinase domain, which is characteristic for serine/threonine-type kinases. We also(More)
A peptide named apisimin was found in honeybee (Apis mellifera L.) royal jelly (RJ). N-terminal sequencing showed that this peptide corresponded to the sequence of a cDNA clone isolated from an expression cDNA library prepared from heads of nurse honeybees. No homology was found between the protein sequence of apisimin with a molecular mass of 5540.4 Da and(More)
From a cDNA sequence, we have deduced the amino acid sequence for a human amyloid precursor-like protein (APPH) with > 92% identity to the CDEI binding protein (CDEBP) of the mouse and the fragmentary rat protein YWK-II of unknown function. Expression of APPH was found in all tissues examined. A striking homology of APPH to human amyloid precursor protein(More)
The human amyloid precursor-like protein APLP2 is a highly conserved homologue of a sequence-specific DNA-binding mouse protein with a predicted function in the cell cycle. Somatic cell hybrids segregating human chromosomes were used to assign the APLP2 gene to chromosome 11. Fluorescence in situ hybridization confirmed this assignment and further localized(More)
The chemical synthesis of a gene coding for a polypeptide of 77 amino acid residues (designated ceaB3) representing a fragment of the CEA-B3 domain of carcinoembryonic antigen (CEA) was achieved. The ceaB3 fragment was cloned into the plasmid pLZPWB1 at the C-terminus of a derivative lacZMF of the lacZ gene, devoid of methionine and cysteine amino acid(More)
Bovine monocyte chemoattractant protein-1 (bovine MCP-1) cDNA has recently been characterized and shown to be highly expressed in bovine seminal vesicles secretory epithelium as well as in phytohemagglutinin (PHA)-stimulated peripheral blood mononuclear leukocytes (PMNLs). In an attempt to isolate the MCP-1 gene, we screened a bovine genomic cosmid library(More)