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Biochemical Genetics (v.36, #3-4)


Distribution of Allelic Forms of Erythrocyte H1 Histones in Japanese Quail Populations Divergently Selected for Amount of Weight Loss After Transient Starvation by Jan Palyga (pp. 79-92).
Three polymorphic subtypes of erythrocytehistone H1 (H1.a, H1.b, and H1.z) were analyzed using asodium dodecyl sulfate polyacrylamide gel in quailpopulations divergently selected for a high (line 1) or low (line 2) reduction in body massfollowing temporary food withdrawal. Both H1.b and H1.zhistone alleles were found to be differently distributedin these populations during the selection period. The frequency of b1 in line 2 wasapproximately 1.9-2.8 times lower than in line 1 andapproached the values in line 1 when the selection wassuspended. Similarly, the frequency of allelez2 at locus H1.z increased significantly (about 1.6-2.3 times)in line 2 during selection and returned to the initialvalues when selection was stopped. On the other hand,allele a0 at locus H1.a was kept atrelatively low levels (usually below 0.05) in both linesduring selection. At that time its level wasapproximately three to four times lower than in a randommating control population. When selection was suspended, the frequency of a0 in line 1increased significantly, approaching the values in thecontrol line, and remained essentially unchanged in line2. Thus, all three polymorphic histone H1 loci in quailresponded through changes in allele frequencies to thebreeding selection, which was directed at the amount ofbody weight loss upon transient starvation. It seemsthat either H1 histone locus could be linked to loci controlling the rate of body weightreduction following starvation or weight loss duringfasting might be influenced by a panel of H1 histonealleles that can contribute to functional differences in avian chromatin.

Keywords: JAPANESE QUAIL; ERYTHROCYTE; HISTONE H1; POLYMORPHISM; SELECTION


Genes for Polymorphic H1 Histones Are Linked in the Japanese Quail Genome by Jan Palyga (pp. 93-103).
In a previous report (Palyga, J., Biochem.Genet. 29, 431-445, 1991), three subtypes oferythrocyte histone H1 were found to vary in a Japanesequail population. While H1.b and H1.z histones were eachrepresented by two electromorphs differing in apparentmolecular weights, a polymorphism of histone H1.a wasconnected with a lack of this protein in some birds. Asa genetic basis for this variability was demonstrated only in H1.b, here genetic data are providedwhich indicate that both H1.a and H1.z are encoded bytwo codominant alleles at a locus. A linkage analysis offamily data in 13 quail pedigrees has revealed a significant linkage between H1.a and H1.z andbetween H1.b and H1.z ( lod scores about 12 and 5,respectively). Thus, a gene for histone H1.z is locatedbetween H1.a and H1.b in the quail genome.

Keywords: JAPANESE QUAIL; ERYTHROCYTE; HISTONE H1; GENETIC LINKAGE


Steroid Binding by Mouse Salivary Proteins by Robert C. Karn (pp. 105-117).
The goals of this study were to determine thesteroid-binding specificity of the mouse salivaryandrogen-binding protein (ABP) family and to ascertainwhether there might be other proteins in mouse saliva capable of binding steroids. The optimalconditions for testosterone binding by mouse salivaryproteins were determined using a small-scalechromatography system to separate bound from unboundsteroid. Testosterone binding appeared to be biphasicbut was directly proportional to saliva concentration,with an optimum temperature of 37 C in the second phase.These results were used to develop a steroid-binding protocol to study the steroid specificity ofsalivary proteins separated by electrophoresis. The ABPfamily bound testosterone and progesterone well andHO-progesterone and DHT to a lesser extent but did not bind either cholesterol or estradiol.Steroid structural comparisons suggest that binding byABP is governed by the A ring of the steroid. Anotherprotein that is not a member of the ABP family bound cholesterol specifically but no protein thatspecifically bound estradiol was observed.

Keywords: ANDROGEN-BINDING PROTEIN; STEROID-BINDING; SALIVARY PROTEINS; SEXUAL SELECTION; ASSORTATIVE MATE SELECTION BEHAVIOR; PHEREMONE


Identification and Cloning of a Truncated Isoform of the Cardiac Sodium-Calcium Exchanger in the BALB/c Mouse Heart by Shundi Shi; Bo Chang; Steven R. Brunnert (pp. 119-135).
A truncated isoform of the cardiacsodium-calcium exchanger (NCX1) was identified andcloned from BALB/c mouse heart. This cDNA clone has anAATAAA polyadenylation signal in the 3′untranslated region that caused the 3344-bp clone to stop at a prematuretermination site and encode for a 940-amino acid (AA)protein, in contrast to the wild-type C57BL/6 mouse,which has a 970-AA protein. Comparing the predicted AA sequence of NCX1 between the two mousestrains by hydropathic plot, we found that the BALB/cNCX1 protein has only 11 extracellular domains, missingone domain at the COOH terminal, while C57BL/6 mice have 12 extracellular domains, similar to otherspecies. Using the mouse mapping gene panel BCB, theNCX1 gene was mapped to the distal end of mousechromosome 17 (51.3 cM), confirming the data published from the rat probe.

Keywords: SODIUM-CALCIUM EXCHANGER HEART BALB; C MOUSE C57BL; MOUSE CLONING


Plasma Esterase (ES) Polymorphism in the Tammar Wallaby, Macropus eugenii by Kevin Bell; Des Cooper; Helen Arthur; W. E. Poole (pp. 137-146).
The major plasma esterase in the tammar wallabywas identified as a carboxylesterase by inhibitionstudies and polymorphism with six variants was observedby isoelectric focusing (pH 4.2-4.9), followed by staining for esterase activity. Familystudies demonstrated an inheritance of six codominantalleles, ESA,B,C,D,E,F, and populationstudies revealed marked differences in the allelefrequencies in five Australian populations of tammar wallabies.

Keywords: PLASMA ESTERASE; CARBOXYLESTERASE; GENETICS; POLYMORPHISM; TAMMAR WALLABY

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